HEADER VIRAL PROTEIN 26-MAR-18 6CUF TITLE CRYO-EM STRUCTURE AT 4.2 A RESOLUTION OF VACCINE-ELICITED ANTIBODY TITLE 2 VFP1.01 IN COMPLEX WITH HIV-1 ENV BG505 DS-SOSIP, AND ANTIBODIES TITLE 3 VRC03 AND PGT122 COMPND MOL_ID: 1; COMPND 2 MOLECULE: VFP1.01 HEAVY CHAIN; COMPND 3 CHAIN: 3, H, h; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: VFP1.01 LIGHT CHAIN; COMPND 7 CHAIN: 4, L, l; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: PGT122 HEAVY CHAIN; COMPND 11 CHAIN: 5, M, m; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: PGT122 LIGHT CHAIN; COMPND 15 CHAIN: 6, N, n; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: VRC03 LIGHT CHAIN; COMPND 19 CHAIN: 7, R, r; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 6; COMPND 22 MOLECULE: VRC03 HEAVY CHAIN; COMPND 23 CHAIN: 8, Q, q; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 7; COMPND 26 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 27 CHAIN: C, 2, d; COMPND 28 ENGINEERED: YES; COMPND 29 MOL_ID: 8; COMPND 30 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 31 CHAIN: D, A, c; COMPND 32 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_COMMON: MOUSE; SOURCE 11 ORGANISM_TAXID: 10090; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 31 ORGANISM_COMMON: HUMAN; SOURCE 32 ORGANISM_TAXID: 9606; SOURCE 33 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 34 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 35 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 36 MOL_ID: 6; SOURCE 37 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 38 ORGANISM_COMMON: HUMAN; SOURCE 39 ORGANISM_TAXID: 9606; SOURCE 40 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 41 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 42 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 43 MOL_ID: 7; SOURCE 44 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 45 ORGANISM_TAXID: 11676; SOURCE 46 GENE: ENV; SOURCE 47 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 48 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 49 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 50 MOL_ID: 8; SOURCE 51 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 52 ORGANISM_TAXID: 11676; SOURCE 53 GENE: ENV; SOURCE 54 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 55 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 56 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1 ENV, BG505 SOSIP, FUSION PEPTIDE, VRC03, PGT122, VFP7.04, VIRAL KEYWDS 2 PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR P.ACHARYA,B.CARRAGHER,C.S.POTTER,P.D.KWONG REVDAT 1 25-JUL-18 6CUF 0 JRNL AUTH A.S.DINGENS,P.ACHARYA,H.K.HADDOX,R.RAWI,K.XU,G.Y.CHUANG, JRNL AUTH 2 H.WEI,B.ZHANG,J.R.MASCOLA,B.CARRAGHER,C.S.POTTER, JRNL AUTH 3 J.OVERBAUGH,P.D.KWONG,J.D.BLOOM JRNL TITL COMPLETE FUNCTIONAL MAPPING OF INFECTION- AND JRNL TITL 2 VACCINE-ELICITED ANTIBODIES AGAINST THE FUSION PEPTIDE OF JRNL TITL 3 HIV. JRNL REF PLOS PATHOG. V. 14 07159 2018 JRNL REFN ESSN 1553-7374 JRNL PMID 29975771 JRNL DOI 10.1371/JOURNAL.PPAT.1007159 REMARK 2 REMARK 2 RESOLUTION. 4.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : LEGINON, GCTF, UCSF CHIMERA, PHENIX, REMARK 3 CRYOSPARC, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT REMARK 3 REFINEMENT TARGET : CORRELATION COEFFICIENT REMARK 3 OVERALL ANISOTROPIC B VALUE : 142.000 REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 4.000 REMARK 3 NUMBER OF PARTICLES : 44652 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 6CUF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-18. REMARK 100 THE DEPOSITION ID IS D_1000233399. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : VFP1.01-BG505 DS-SOSIP-VRC03 REMARK 245 -PGT122; PGT122; VRC03; VFP1.01; REMARK 245 BG505 DS-SOSIP REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.50 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 864 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : NULL REMARK 245 MAXIMUM DEFOCUS (NM) : NULL REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 70.28 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : 130000 REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 24-MERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 3, 4, 5, 6, 7, 8, C, D, H, L, REMARK 350 AND CHAINS: M, N, Q, R, h, l, m, n, q, REMARK 350 AND CHAINS: r, 2, A, c, d REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER 3 112 REMARK 465 PRO 3 113 REMARK 465 ALA 3 114 REMARK 465 SER 3 115 REMARK 465 THR 3 116 REMARK 465 LYS 3 117 REMARK 465 GLY 3 118 REMARK 465 PRO 3 119 REMARK 465 SER 3 120 REMARK 465 VAL 3 121 REMARK 465 PHE 3 122 REMARK 465 PRO 3 123 REMARK 465 LEU 3 124 REMARK 465 ALA 3 125 REMARK 465 PRO 3 126 REMARK 465 GLY 3 127 REMARK 465 THR 3 128 REMARK 465 ALA 3 129 REMARK 465 ALA 3 130 REMARK 465 LEU 3 131 REMARK 465 GLY 3 132 REMARK 465 CYS 3 133 REMARK 465 LEU 3 134 REMARK 465 VAL 3 135 REMARK 465 LYS 3 136 REMARK 465 ASP 3 137 REMARK 465 TYR 3 138 REMARK 465 PHE 3 139 REMARK 465 PRO 3 140 REMARK 465 GLU 3 141 REMARK 465 PRO 3 142 REMARK 465 VAL 3 143 REMARK 465 THR 3 144 REMARK 465 VAL 3 145 REMARK 465 SER 3 146 REMARK 465 TRP 3 147 REMARK 465 ASN 3 148 REMARK 465 SER 3 149 REMARK 465 GLY 3 150 REMARK 465 ALA 3 151 REMARK 465 LEU 3 152 REMARK 465 THR 3 153 REMARK 465 SER 3 154 REMARK 465 GLY 3 155 REMARK 465 VAL 3 156 REMARK 465 HIS 3 157 REMARK 465 THR 3 158 REMARK 465 PHE 3 159 REMARK 465 PRO 3 160 REMARK 465 ALA 3 161 REMARK 465 VAL 3 162 REMARK 465 LEU 3 163 REMARK 465 GLN 3 164 REMARK 465 SER 3 165 REMARK 465 SER 3 166 REMARK 465 GLY 3 167 REMARK 465 LEU 3 168 REMARK 465 TYR 3 169 REMARK 465 SER 3 170 REMARK 465 LEU 3 171 REMARK 465 SER 3 172 REMARK 465 SER 3 173 REMARK 465 VAL 3 174 REMARK 465 VAL 3 175 REMARK 465 THR 3 176 REMARK 465 VAL 3 177 REMARK 465 PRO 3 178 REMARK 465 SER 3 179 REMARK 465 SER 3 180 REMARK 465 SER 3 181 REMARK 465 LEU 3 182 REMARK 465 GLY 3 183 REMARK 465 THR 3 184 REMARK 465 GLN 3 185 REMARK 465 THR 3 186 REMARK 465 TYR 3 187 REMARK 465 ILE 3 188 REMARK 465 CYS 3 189 REMARK 465 ASN 3 190 REMARK 465 VAL 3 191 REMARK 465 ASN 3 192 REMARK 465 HIS 3 193 REMARK 465 LYS 3 194 REMARK 465 PRO 3 195 REMARK 465 SER 3 196 REMARK 465 ASN 3 197 REMARK 465 THR 3 198 REMARK 465 LYS 3 199 REMARK 465 VAL 3 200 REMARK 465 ASP 3 201 REMARK 465 LYS 3 202 REMARK 465 LYS 3 203 REMARK 465 VAL 3 204 REMARK 465 GLU 3 205 REMARK 465 PRO 3 206 REMARK 465 THR 4 114 REMARK 465 VAL 4 115 REMARK 465 ALA 4 116 REMARK 465 ALA 4 117 REMARK 465 PRO 4 118 REMARK 465 SER 4 119 REMARK 465 VAL 4 120 REMARK 465 PHE 4 121 REMARK 465 ILE 4 122 REMARK 465 PHE 4 123 REMARK 465 PRO 4 124 REMARK 465 PRO 4 125 REMARK 465 SER 4 126 REMARK 465 ASP 4 127 REMARK 465 GLU 4 128 REMARK 465 GLN 4 129 REMARK 465 LEU 4 130 REMARK 465 LYS 4 131 REMARK 465 SER 4 132 REMARK 465 GLY 4 133 REMARK 465 THR 4 134 REMARK 465 ALA 4 135 REMARK 465 SER 4 136 REMARK 465 VAL 4 137 REMARK 465 VAL 4 138 REMARK 465 CYS 4 139 REMARK 465 LEU 4 140 REMARK 465 LEU 4 141 REMARK 465 ASN 4 142 REMARK 465 ASN 4 143 REMARK 465 PHE 4 144 REMARK 465 TYR 4 145 REMARK 465 PRO 4 146 REMARK 465 ARG 4 147 REMARK 465 GLU 4 148 REMARK 465 ALA 4 149 REMARK 465 LYS 4 150 REMARK 465 VAL 4 151 REMARK 465 GLN 4 152 REMARK 465 TRP 4 153 REMARK 465 LYS 4 154 REMARK 465 VAL 4 155 REMARK 465 ASP 4 156 REMARK 465 ASN 4 157 REMARK 465 ALA 4 158 REMARK 465 LEU 4 159 REMARK 465 GLN 4 160 REMARK 465 SER 4 161 REMARK 465 GLY 4 162 REMARK 465 ASN 4 163 REMARK 465 SER 4 164 REMARK 465 GLN 4 165 REMARK 465 GLU 4 166 REMARK 465 SER 4 167 REMARK 465 VAL 4 168 REMARK 465 THR 4 169 REMARK 465 GLU 4 170 REMARK 465 GLN 4 171 REMARK 465 ASP 4 172 REMARK 465 SER 4 173 REMARK 465 LYS 4 174 REMARK 465 ASP 4 175 REMARK 465 SER 4 176 REMARK 465 THR 4 177 REMARK 465 TYR 4 178 REMARK 465 SER 4 179 REMARK 465 LEU 4 180 REMARK 465 SER 4 181 REMARK 465 SER 4 182 REMARK 465 THR 4 183 REMARK 465 LEU 4 184 REMARK 465 THR 4 185 REMARK 465 LEU 4 186 REMARK 465 SER 4 187 REMARK 465 LYS 4 188 REMARK 465 ALA 4 189 REMARK 465 ASP 4 190 REMARK 465 TYR 4 191 REMARK 465 GLU 4 192 REMARK 465 LYS 4 193 REMARK 465 HIS 4 194 REMARK 465 LYS 4 195 REMARK 465 VAL 4 196 REMARK 465 TYR 4 197 REMARK 465 ALA 4 198 REMARK 465 CYS 4 199 REMARK 465 GLU 4 200 REMARK 465 VAL 4 201 REMARK 465 THR 4 202 REMARK 465 HIS 4 203 REMARK 465 GLN 4 204 REMARK 465 GLY 4 205 REMARK 465 LEU 4 206 REMARK 465 SER 4 207 REMARK 465 SER 4 208 REMARK 465 PRO 4 209 REMARK 465 VAL 4 210 REMARK 465 THR 4 211 REMARK 465 LYS 4 212 REMARK 465 SER 4 213 REMARK 465 PHE 4 214 REMARK 465 ASN 4 215 REMARK 465 ARG 4 216 REMARK 465 GLY 4 217 REMARK 465 GLU 4 218 REMARK 465 CYS 4 219 REMARK 465 GLU C 185A REMARK 465 ASN C 185B REMARK 465 GLN C 185C REMARK 465 GLY C 185D REMARK 465 ASN C 185E REMARK 465 ARG C 185F REMARK 465 SER C 185G REMARK 465 ASN C 185H REMARK 465 ASN C 185I REMARK 465 THR C 400 REMARK 465 SER C 401 REMARK 465 VAL C 402 REMARK 465 GLN C 403 REMARK 465 GLY C 404 REMARK 465 SER C 405 REMARK 465 ASN C 406 REMARK 465 SER C 407 REMARK 465 THR C 408 REMARK 465 GLY C 409 REMARK 465 SER C 410 REMARK 465 ILE D 548 REMARK 465 VAL D 549 REMARK 465 GLN D 550 REMARK 465 GLN D 551 REMARK 465 GLN D 552 REMARK 465 SER D 553 REMARK 465 ASN D 554 REMARK 465 LEU D 555 REMARK 465 LEU D 556 REMARK 465 ARG D 557 REMARK 465 ALA D 558 REMARK 465 ILE D 559 REMARK 465 GLU D 560 REMARK 465 ALA D 561 REMARK 465 GLN D 562 REMARK 465 GLN D 563 REMARK 465 HIS D 564 REMARK 465 LEU D 565 REMARK 465 LEU D 566 REMARK 465 LYS D 567 REMARK 465 LEU D 568 REMARK 465 SER H 112 REMARK 465 PRO H 113 REMARK 465 ALA H 114 REMARK 465 SER H 115 REMARK 465 THR H 116 REMARK 465 LYS H 117 REMARK 465 GLY H 118 REMARK 465 PRO H 119 REMARK 465 SER H 120 REMARK 465 VAL H 121 REMARK 465 PHE H 122 REMARK 465 PRO H 123 REMARK 465 LEU H 124 REMARK 465 ALA H 125 REMARK 465 PRO H 126 REMARK 465 GLY H 127 REMARK 465 THR H 128 REMARK 465 ALA H 129 REMARK 465 ALA H 130 REMARK 465 LEU H 131 REMARK 465 GLY H 132 REMARK 465 CYS H 133 REMARK 465 LEU H 134 REMARK 465 VAL H 135 REMARK 465 LYS H 136 REMARK 465 ASP H 137 REMARK 465 TYR H 138 REMARK 465 PHE H 139 REMARK 465 PRO H 140 REMARK 465 GLU H 141 REMARK 465 PRO H 142 REMARK 465 VAL H 143 REMARK 465 THR H 144 REMARK 465 VAL H 145 REMARK 465 SER H 146 REMARK 465 TRP H 147 REMARK 465 ASN H 148 REMARK 465 SER H 149 REMARK 465 GLY H 150 REMARK 465 ALA H 151 REMARK 465 LEU H 152 REMARK 465 THR H 153 REMARK 465 SER H 154 REMARK 465 GLY H 155 REMARK 465 VAL H 156 REMARK 465 HIS H 157 REMARK 465 THR H 158 REMARK 465 PHE H 159 REMARK 465 PRO H 160 REMARK 465 ALA H 161 REMARK 465 VAL H 162 REMARK 465 LEU H 163 REMARK 465 GLN H 164 REMARK 465 SER H 165 REMARK 465 SER H 166 REMARK 465 GLY H 167 REMARK 465 LEU H 168 REMARK 465 TYR H 169 REMARK 465 SER H 170 REMARK 465 LEU H 171 REMARK 465 SER H 172 REMARK 465 SER H 173 REMARK 465 VAL H 174 REMARK 465 VAL H 175 REMARK 465 THR H 176 REMARK 465 VAL H 177 REMARK 465 PRO H 178 REMARK 465 SER H 179 REMARK 465 SER H 180 REMARK 465 SER H 181 REMARK 465 LEU H 182 REMARK 465 GLY H 183 REMARK 465 THR H 184 REMARK 465 GLN H 185 REMARK 465 THR H 186 REMARK 465 TYR H 187 REMARK 465 ILE H 188 REMARK 465 CYS H 189 REMARK 465 ASN H 190 REMARK 465 VAL H 191 REMARK 465 ASN H 192 REMARK 465 HIS H 193 REMARK 465 LYS H 194 REMARK 465 PRO H 195 REMARK 465 SER H 196 REMARK 465 ASN H 197 REMARK 465 THR H 198 REMARK 465 LYS H 199 REMARK 465 VAL H 200 REMARK 465 ASP H 201 REMARK 465 LYS H 202 REMARK 465 LYS H 203 REMARK 465 VAL H 204 REMARK 465 GLU H 205 REMARK 465 PRO H 206 REMARK 465 THR L 114 REMARK 465 VAL L 115 REMARK 465 ALA L 116 REMARK 465 ALA L 117 REMARK 465 PRO L 118 REMARK 465 SER L 119 REMARK 465 VAL L 120 REMARK 465 PHE L 121 REMARK 465 ILE L 122 REMARK 465 PHE L 123 REMARK 465 PRO L 124 REMARK 465 PRO L 125 REMARK 465 SER L 126 REMARK 465 ASP L 127 REMARK 465 GLU L 128 REMARK 465 GLN L 129 REMARK 465 LEU L 130 REMARK 465 LYS L 131 REMARK 465 SER L 132 REMARK 465 GLY L 133 REMARK 465 THR L 134 REMARK 465 ALA L 135 REMARK 465 SER L 136 REMARK 465 VAL L 137 REMARK 465 VAL L 138 REMARK 465 CYS L 139 REMARK 465 LEU L 140 REMARK 465 LEU L 141 REMARK 465 ASN L 142 REMARK 465 ASN L 143 REMARK 465 PHE L 144 REMARK 465 TYR L 145 REMARK 465 PRO L 146 REMARK 465 ARG L 147 REMARK 465 GLU L 148 REMARK 465 ALA L 149 REMARK 465 LYS L 150 REMARK 465 VAL L 151 REMARK 465 GLN L 152 REMARK 465 TRP L 153 REMARK 465 LYS L 154 REMARK 465 VAL L 155 REMARK 465 ASP L 156 REMARK 465 ASN L 157 REMARK 465 ALA L 158 REMARK 465 LEU L 159 REMARK 465 GLN L 160 REMARK 465 SER L 161 REMARK 465 GLY L 162 REMARK 465 ASN L 163 REMARK 465 SER L 164 REMARK 465 GLN L 165 REMARK 465 GLU L 166 REMARK 465 SER L 167 REMARK 465 VAL L 168 REMARK 465 THR L 169 REMARK 465 GLU L 170 REMARK 465 GLN L 171 REMARK 465 ASP L 172 REMARK 465 SER L 173 REMARK 465 LYS L 174 REMARK 465 ASP L 175 REMARK 465 SER L 176 REMARK 465 THR L 177 REMARK 465 TYR L 178 REMARK 465 SER L 179 REMARK 465 LEU L 180 REMARK 465 SER L 181 REMARK 465 SER L 182 REMARK 465 THR L 183 REMARK 465 LEU L 184 REMARK 465 THR L 185 REMARK 465 LEU L 186 REMARK 465 SER L 187 REMARK 465 LYS L 188 REMARK 465 ALA L 189 REMARK 465 ASP L 190 REMARK 465 TYR L 191 REMARK 465 GLU L 192 REMARK 465 LYS L 193 REMARK 465 HIS L 194 REMARK 465 LYS L 195 REMARK 465 VAL L 196 REMARK 465 TYR L 197 REMARK 465 ALA L 198 REMARK 465 CYS L 199 REMARK 465 GLU L 200 REMARK 465 VAL L 201 REMARK 465 THR L 202 REMARK 465 HIS L 203 REMARK 465 GLN L 204 REMARK 465 GLY L 205 REMARK 465 LEU L 206 REMARK 465 SER L 207 REMARK 465 SER L 208 REMARK 465 PRO L 209 REMARK 465 VAL L 210 REMARK 465 THR L 211 REMARK 465 LYS L 212 REMARK 465 SER L 213 REMARK 465 PHE L 214 REMARK 465 ASN L 215 REMARK 465 ARG L 216 REMARK 465 GLY L 217 REMARK 465 GLU L 218 REMARK 465 CYS L 219 REMARK 465 SER h 112 REMARK 465 PRO h 113 REMARK 465 ALA h 114 REMARK 465 SER h 115 REMARK 465 THR h 116 REMARK 465 LYS h 117 REMARK 465 GLY h 118 REMARK 465 PRO h 119 REMARK 465 SER h 120 REMARK 465 VAL h 121 REMARK 465 PHE h 122 REMARK 465 PRO h 123 REMARK 465 LEU h 124 REMARK 465 ALA h 125 REMARK 465 PRO h 126 REMARK 465 GLY h 127 REMARK 465 THR h 128 REMARK 465 ALA h 129 REMARK 465 ALA h 130 REMARK 465 LEU h 131 REMARK 465 GLY h 132 REMARK 465 CYS h 133 REMARK 465 LEU h 134 REMARK 465 VAL h 135 REMARK 465 LYS h 136 REMARK 465 ASP h 137 REMARK 465 TYR h 138 REMARK 465 PHE h 139 REMARK 465 PRO h 140 REMARK 465 GLU h 141 REMARK 465 PRO h 142 REMARK 465 VAL h 143 REMARK 465 THR h 144 REMARK 465 VAL h 145 REMARK 465 SER h 146 REMARK 465 TRP h 147 REMARK 465 ASN h 148 REMARK 465 SER h 149 REMARK 465 GLY h 150 REMARK 465 ALA h 151 REMARK 465 LEU h 152 REMARK 465 THR h 153 REMARK 465 SER h 154 REMARK 465 GLY h 155 REMARK 465 VAL h 156 REMARK 465 HIS h 157 REMARK 465 THR h 158 REMARK 465 PHE h 159 REMARK 465 PRO h 160 REMARK 465 ALA h 161 REMARK 465 VAL h 162 REMARK 465 LEU h 163 REMARK 465 GLN h 164 REMARK 465 SER h 165 REMARK 465 SER h 166 REMARK 465 GLY h 167 REMARK 465 LEU h 168 REMARK 465 TYR h 169 REMARK 465 SER h 170 REMARK 465 LEU h 171 REMARK 465 SER h 172 REMARK 465 SER h 173 REMARK 465 VAL h 174 REMARK 465 VAL h 175 REMARK 465 THR h 176 REMARK 465 VAL h 177 REMARK 465 PRO h 178 REMARK 465 SER h 179 REMARK 465 SER h 180 REMARK 465 SER h 181 REMARK 465 LEU h 182 REMARK 465 GLY h 183 REMARK 465 THR h 184 REMARK 465 GLN h 185 REMARK 465 THR h 186 REMARK 465 TYR h 187 REMARK 465 ILE h 188 REMARK 465 CYS h 189 REMARK 465 ASN h 190 REMARK 465 VAL h 191 REMARK 465 ASN h 192 REMARK 465 HIS h 193 REMARK 465 LYS h 194 REMARK 465 PRO h 195 REMARK 465 SER h 196 REMARK 465 ASN h 197 REMARK 465 THR h 198 REMARK 465 LYS h 199 REMARK 465 VAL h 200 REMARK 465 ASP h 201 REMARK 465 LYS h 202 REMARK 465 LYS h 203 REMARK 465 VAL h 204 REMARK 465 GLU h 205 REMARK 465 PRO h 206 REMARK 465 THR l 114 REMARK 465 VAL l 115 REMARK 465 ALA l 116 REMARK 465 ALA l 117 REMARK 465 PRO l 118 REMARK 465 SER l 119 REMARK 465 VAL l 120 REMARK 465 PHE l 121 REMARK 465 ILE l 122 REMARK 465 PHE l 123 REMARK 465 PRO l 124 REMARK 465 PRO l 125 REMARK 465 SER l 126 REMARK 465 ASP l 127 REMARK 465 GLU l 128 REMARK 465 GLN l 129 REMARK 465 LEU l 130 REMARK 465 LYS l 131 REMARK 465 SER l 132 REMARK 465 GLY l 133 REMARK 465 THR l 134 REMARK 465 ALA l 135 REMARK 465 SER l 136 REMARK 465 VAL l 137 REMARK 465 VAL l 138 REMARK 465 CYS l 139 REMARK 465 LEU l 140 REMARK 465 LEU l 141 REMARK 465 ASN l 142 REMARK 465 ASN l 143 REMARK 465 PHE l 144 REMARK 465 TYR l 145 REMARK 465 PRO l 146 REMARK 465 ARG l 147 REMARK 465 GLU l 148 REMARK 465 ALA l 149 REMARK 465 LYS l 150 REMARK 465 VAL l 151 REMARK 465 GLN l 152 REMARK 465 TRP l 153 REMARK 465 LYS l 154 REMARK 465 VAL l 155 REMARK 465 ASP l 156 REMARK 465 ASN l 157 REMARK 465 ALA l 158 REMARK 465 LEU l 159 REMARK 465 GLN l 160 REMARK 465 SER l 161 REMARK 465 GLY l 162 REMARK 465 ASN l 163 REMARK 465 SER l 164 REMARK 465 GLN l 165 REMARK 465 GLU l 166 REMARK 465 SER l 167 REMARK 465 VAL l 168 REMARK 465 THR l 169 REMARK 465 GLU l 170 REMARK 465 GLN l 171 REMARK 465 ASP l 172 REMARK 465 SER l 173 REMARK 465 LYS l 174 REMARK 465 ASP l 175 REMARK 465 SER l 176 REMARK 465 THR l 177 REMARK 465 TYR l 178 REMARK 465 SER l 179 REMARK 465 LEU l 180 REMARK 465 SER l 181 REMARK 465 SER l 182 REMARK 465 THR l 183 REMARK 465 LEU l 184 REMARK 465 THR l 185 REMARK 465 LEU l 186 REMARK 465 SER l 187 REMARK 465 LYS l 188 REMARK 465 ALA l 189 REMARK 465 ASP l 190 REMARK 465 TYR l 191 REMARK 465 GLU l 192 REMARK 465 LYS l 193 REMARK 465 HIS l 194 REMARK 465 LYS l 195 REMARK 465 VAL l 196 REMARK 465 TYR l 197 REMARK 465 ALA l 198 REMARK 465 CYS l 199 REMARK 465 GLU l 200 REMARK 465 VAL l 201 REMARK 465 THR l 202 REMARK 465 HIS l 203 REMARK 465 GLN l 204 REMARK 465 GLY l 205 REMARK 465 LEU l 206 REMARK 465 SER l 207 REMARK 465 SER l 208 REMARK 465 PRO l 209 REMARK 465 VAL l 210 REMARK 465 THR l 211 REMARK 465 LYS l 212 REMARK 465 SER l 213 REMARK 465 PHE l 214 REMARK 465 ASN l 215 REMARK 465 ARG l 216 REMARK 465 GLY l 217 REMARK 465 GLU l 218 REMARK 465 CYS l 219 REMARK 465 GLU 2 185A REMARK 465 ASN 2 185B REMARK 465 GLN 2 185C REMARK 465 GLY 2 185D REMARK 465 ASN 2 185E REMARK 465 ARG 2 185F REMARK 465 SER 2 185G REMARK 465 ASN 2 185H REMARK 465 ASN 2 185I REMARK 465 THR 2 400 REMARK 465 SER 2 401 REMARK 465 VAL 2 402 REMARK 465 GLN 2 403 REMARK 465 GLY 2 404 REMARK 465 SER 2 405 REMARK 465 ASN 2 406 REMARK 465 SER 2 407 REMARK 465 THR 2 408 REMARK 465 GLY 2 409 REMARK 465 SER 2 410 REMARK 465 ILE A 548 REMARK 465 VAL A 549 REMARK 465 GLN A 550 REMARK 465 GLN A 551 REMARK 465 GLN A 552 REMARK 465 SER A 553 REMARK 465 ASN A 554 REMARK 465 LEU A 555 REMARK 465 LEU A 556 REMARK 465 ARG A 557 REMARK 465 ALA A 558 REMARK 465 ILE A 559 REMARK 465 GLU A 560 REMARK 465 ALA A 561 REMARK 465 GLN A 562 REMARK 465 GLN A 563 REMARK 465 HIS A 564 REMARK 465 LEU A 565 REMARK 465 LEU A 566 REMARK 465 LYS A 567 REMARK 465 LEU A 568 REMARK 465 ILE c 548 REMARK 465 VAL c 549 REMARK 465 GLN c 550 REMARK 465 GLN c 551 REMARK 465 GLN c 552 REMARK 465 SER c 553 REMARK 465 ASN c 554 REMARK 465 LEU c 555 REMARK 465 LEU c 556 REMARK 465 ARG c 557 REMARK 465 ALA c 558 REMARK 465 ILE c 559 REMARK 465 GLU c 560 REMARK 465 ALA c 561 REMARK 465 GLN c 562 REMARK 465 GLN c 563 REMARK 465 HIS c 564 REMARK 465 LEU c 565 REMARK 465 LEU c 566 REMARK 465 LYS c 567 REMARK 465 LEU c 568 REMARK 465 GLU d 185A REMARK 465 ASN d 185B REMARK 465 GLN d 185C REMARK 465 GLY d 185D REMARK 465 ASN d 185E REMARK 465 ARG d 185F REMARK 465 SER d 185G REMARK 465 ASN d 185H REMARK 465 ASN d 185I REMARK 465 THR d 400 REMARK 465 SER d 401 REMARK 465 VAL d 402 REMARK 465 GLN d 403 REMARK 465 GLY d 404 REMARK 465 SER d 405 REMARK 465 ASN d 406 REMARK 465 SER d 407 REMARK 465 THR d 408 REMARK 465 GLY d 409 REMARK 465 SER d 410 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 ND2 ASN 2 160 O5 NAG 2 610 1.51 REMARK 500 ND2 ASN C 160 O5 NAG C 610 1.51 REMARK 500 ND2 ASN d 160 O5 NAG d 610 1.51 REMARK 500 ND2 ASN d 392 O5 NAG d 637 1.66 REMARK 500 ND2 ASN C 392 O5 NAG C 637 1.66 REMARK 500 ND2 ASN 2 392 O5 NAG 2 637 1.66 REMARK 500 ND2 ASN C 156 O5 NAG C 606 1.73 REMARK 500 ND2 ASN d 301 O5 NAG d 626 1.79 REMARK 500 ND2 ASN C 301 O5 NAG C 626 1.79 REMARK 500 ND2 ASN 2 301 O5 NAG 2 626 1.79 REMARK 500 ND2 ASN C 355 O5 NAG C 628 1.83 REMARK 500 ND2 ASN d 355 O5 NAG d 628 1.83 REMARK 500 ND2 ASN 2 355 O5 NAG 2 628 1.83 REMARK 500 ND2 ASN 2 295 C1 NAG 2 624 1.85 REMARK 500 ND2 ASN d 295 C1 NAG d 624 1.85 REMARK 500 ND2 ASN C 295 C1 NAG C 624 1.85 REMARK 500 ND2 ASN d 137 O5 NAG d 602 2.00 REMARK 500 ND2 ASN C 137 O5 NAG C 602 2.00 REMARK 500 ND2 ASN 2 137 O5 NAG 2 602 2.00 REMARK 500 OE2 GLU 2 164 NH1 ARG 2 308 2.02 REMARK 500 OE2 GLU C 164 NH1 ARG C 308 2.02 REMARK 500 OE2 GLU d 164 NH1 ARG d 308 2.02 REMARK 500 ND2 ASN d 363 C2 NAG d 629 2.02 REMARK 500 ND2 ASN 2 363 C2 NAG 2 629 2.02 REMARK 500 ND2 ASN C 363 C2 NAG C 629 2.02 REMARK 500 ND2 ASN d 197 O5 NAG d 613 2.03 REMARK 500 ND2 ASN C 197 O5 NAG C 613 2.03 REMARK 500 ND2 ASN 2 197 O5 NAG 2 613 2.04 REMARK 500 ND2 ASN 2 386 C2 NAG 2 632 2.05 REMARK 500 ND2 ASN C 386 C2 NAG C 632 2.05 REMARK 500 ND2 ASN d 386 C2 NAG d 632 2.05 REMARK 500 CG ASN 2 276 C1 NAG 2 650 2.05 REMARK 500 CG ASN C 276 C1 NAG C 650 2.05 REMARK 500 CG ASN d 276 C1 NAG d 650 2.05 REMARK 500 OG SER L 70 NH1 ARG L 79 2.08 REMARK 500 OG SER l 70 NH1 ARG l 79 2.09 REMARK 500 OG SER 4 70 NH1 ARG 4 79 2.09 REMARK 500 CG ASN 2 355 C1 NAG 2 628 2.09 REMARK 500 CG ASN C 355 C1 NAG C 628 2.09 REMARK 500 CG ASN d 355 C1 NAG d 628 2.09 REMARK 500 CG ASN C 156 C1 NAG C 606 2.09 REMARK 500 OD1 ASN d 295 C1 NAG d 624 2.12 REMARK 500 OD1 ASN C 295 C1 NAG C 624 2.12 REMARK 500 OD1 ASN 2 295 C1 NAG 2 624 2.12 REMARK 500 CG ASN C 392 C1 NAG C 637 2.12 REMARK 500 CG ASN 2 392 C1 NAG 2 637 2.12 REMARK 500 CG ASN d 392 C1 NAG d 637 2.12 REMARK 500 ND2 ASN C 133 O5 NAG C 601 2.13 REMARK 500 ND2 ASN 2 133 O5 NAG 2 601 2.13 REMARK 500 ND2 ASN d 133 O5 NAG d 601 2.13 REMARK 500 REMARK 500 THIS ENTRY HAS 61 CLOSE CONTACTS REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LEU C 494 CA - CB - CG ANGL. DEV. = 19.2 DEGREES REMARK 500 LEU 2 494 CA - CB - CG ANGL. DEV. = 19.3 DEGREES REMARK 500 LEU d 494 CA - CB - CG ANGL. DEV. = 19.2 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU 4 52 -61.04 -90.30 REMARK 500 LYS 4 55 76.32 57.41 REMARK 500 THR 4 74 -50.45 -121.08 REMARK 500 SER 5 54 62.38 61.49 REMARK 500 LYS 5 64 -11.66 71.51 REMARK 500 SER 5 65 -36.87 -130.31 REMARK 500 GLU 5 100I 56.38 -91.66 REMARK 500 ASN 6 50 -165.87 -123.63 REMARK 500 ASN 6 52 44.97 -142.01 REMARK 500 PHE 6 62 73.93 -100.58 REMARK 500 THR 7 51 -10.62 71.01 REMARK 500 SER 7 52 -4.66 -142.19 REMARK 500 LYS 7 77 70.99 58.44 REMARK 500 PRO 8 100E 81.41 -65.02 REMARK 500 ASN C 80 63.88 29.88 REMARK 500 MET C 100 -5.66 67.12 REMARK 500 THR C 163 -167.40 -124.18 REMARK 500 ASN C 188 -168.82 -79.91 REMARK 500 GLU C 268 -50.14 -123.34 REMARK 500 PHE C 391 49.99 -94.03 REMARK 500 SER D 546 -31.06 -130.96 REMARK 500 LEU D 602 -10.61 71.99 REMARK 500 ASN D 616 45.58 35.81 REMARK 500 GLN D 640 -7.03 73.36 REMARK 500 SER H 87 98.61 -67.85 REMARK 500 LYS L 55 74.61 55.79 REMARK 500 SER M 54 62.34 61.83 REMARK 500 LYS M 64 -14.20 70.15 REMARK 500 SER M 65 -36.39 -132.44 REMARK 500 ASN N 50 -168.01 -115.20 REMARK 500 ASN N 52 45.03 -142.06 REMARK 500 ASP N 60 -164.55 -79.84 REMARK 500 PRO Q 100E 84.38 -65.98 REMARK 500 LEU R 47 -60.89 -97.27 REMARK 500 THR R 51 -11.09 71.03 REMARK 500 SER R 52 -4.08 -142.51 REMARK 500 LYS R 77 70.28 58.67 REMARK 500 ILE h 48 -61.99 -91.54 REMARK 500 LEU l 52 -60.35 -93.09 REMARK 500 LYS l 55 75.26 57.34 REMARK 500 SER m 54 62.65 61.56 REMARK 500 LYS m 64 -13.14 71.04 REMARK 500 SER m 65 -36.69 -131.29 REMARK 500 GLU m 100I 59.86 -91.28 REMARK 500 ASN n 50 -165.68 -123.83 REMARK 500 ASN n 52 44.70 -142.17 REMARK 500 ASP n 60 -164.94 -79.86 REMARK 500 PHE n 62 74.23 -100.58 REMARK 500 PRO q 100E 84.01 -66.53 REMARK 500 THR r 51 -10.63 71.25 REMARK 500 REMARK 500 THIS ENTRY HAS 72 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 LYS 4 55 VAL 4 56 -140.73 REMARK 500 GLN 7 90 PHE 7 91 -147.09 REMARK 500 LYS L 55 VAL L 56 -141.25 REMARK 500 GLN R 90 PHE R 91 -144.78 REMARK 500 LYS l 55 VAL l 56 -140.87 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG C 624 REMARK 610 NAG 2 624 REMARK 610 NAG d 624 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG 2 601 bound REMARK 800 to ASN 2 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG 2 601 bound REMARK 800 to ASN 2 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 602 through MAN 2 605 bound to ASN 2 137 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 606 through MAN 2 609 bound to ASN 2 156 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 610 through BMA 2 612 bound to ASN 2 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 613 through NAG 2 614 bound to ASN 2 197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 615 through BMA 2 617 bound to ASN 2 234 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 618 through MAN 2 623 bound to ASN 2 262 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 650 through MAN 2 653 bound to ASN 2 276 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 626 through NAG 2 627 bound to ASN 2 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 639 through MAN 2 647 bound to ASN 2 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG 2 628 bound REMARK 800 to ASN 2 355 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 629 through BMA 2 631 bound to ASN 2 363 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 632 through MAN 2 636 bound to ASN 2 386 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 637 through NAG 2 638 bound to ASN 2 392 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 648 through NAG 2 649 bound to ASN 2 448 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 701 bound REMARK 800 to ASN A 637 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 601 bound REMARK 800 to ASN C 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 601 bound REMARK 800 to ASN C 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 602 through MAN C 605 bound to ASN C 137 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 606 through MAN C 609 bound to ASN C 156 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 610 through BMA C 612 bound to ASN C 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 613 through NAG C 614 bound to ASN C 197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 615 through BMA C 617 bound to ASN C 234 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 618 through MAN C 623 bound to ASN C 262 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 650 through MAN C 653 bound to ASN C 276 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 626 through NAG C 627 bound to ASN C 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 639 through MAN C 647 bound to ASN C 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 628 bound REMARK 800 to ASN C 355 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 629 through BMA C 631 bound to ASN C 363 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 632 through MAN C 636 bound to ASN C 386 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 637 through NAG C 638 bound to ASN C 392 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 648 through NAG C 649 bound to ASN C 448 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 701 bound REMARK 800 to ASN D 637 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG c 701 bound REMARK 800 to ASN c 637 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG d 601 bound REMARK 800 to ASN d 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG d 601 bound REMARK 800 to ASN d 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG d REMARK 800 602 through MAN d 605 bound to ASN d 137 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG d REMARK 800 606 through MAN d 609 bound to ASN d 156 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG d REMARK 800 610 through BMA d 612 bound to ASN d 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG d REMARK 800 613 through NAG d 614 bound to ASN d 197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG d REMARK 800 615 through BMA d 617 bound to ASN d 234 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG d REMARK 800 618 through MAN d 623 bound to ASN d 262 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG d REMARK 800 650 through MAN d 653 bound to ASN d 276 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG d REMARK 800 626 through NAG d 627 bound to ASN d 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG d REMARK 800 639 through MAN d 647 bound to ASN d 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG d 628 bound REMARK 800 to ASN d 355 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG d REMARK 800 629 through BMA d 631 bound to ASN d 363 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG d REMARK 800 632 through MAN d 636 bound to ASN d 386 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG d REMARK 800 637 through NAG d 638 bound to ASN d 392 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG d REMARK 800 648 through NAG d 649 bound to ASN d 448 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 624 through NAG 2 625 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 624 through NAG C 625 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG d REMARK 800 624 through NAG d 625 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-7622 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE AT 4.0 A RESOLUTION OF VACCINE-ELICITED ANTIBODY REMARK 900 VFP1.01 IN COMPLEX WITH HIV-1 ENV BG505 DS-SOSIP, AND ANTIBODIES REMARK 900 VRC03 AND PGT122 DBREF 6CUF 3 1 206 PDB 6CUF 6CUF 1 206 DBREF 6CUF 4 1 219 PDB 6CUF 6CUF 1 219 DBREF 6CUF 5 1 111 PDB 6CUF 6CUF 1 111 DBREF 6CUF 6 8 107 PDB 6CUF 6CUF 8 107 DBREF 6CUF 7 1 107 PDB 6CUF 6CUF 1 107 DBREF 6CUF 8 1 111 PDB 6CUF 6CUF 1 111 DBREF 6CUF C 31 505 UNP Q2N0S6 Q2N0S6_9HIV1 30 502 DBREF 6CUF D 512 664 UNP Q2N0S7 Q2N0S7_9HIV1 509 661 DBREF 6CUF H 1 206 PDB 6CUF 6CUF 1 206 DBREF 6CUF L 1 219 PDB 6CUF 6CUF 1 219 DBREF 6CUF M 1 111 PDB 6CUF 6CUF 1 111 DBREF 6CUF N 8 107 PDB 6CUF 6CUF 8 107 DBREF 6CUF Q 1 111 PDB 6CUF 6CUF 1 111 DBREF 6CUF R 1 107 PDB 6CUF 6CUF 1 107 DBREF 6CUF h 1 206 PDB 6CUF 6CUF 1 206 DBREF 6CUF l 1 219 PDB 6CUF 6CUF 1 219 DBREF 6CUF m 1 111 PDB 6CUF 6CUF 1 111 DBREF 6CUF n 8 107 PDB 6CUF 6CUF 8 107 DBREF 6CUF q 1 111 PDB 6CUF 6CUF 1 111 DBREF 6CUF r 1 107 PDB 6CUF 6CUF 1 107 DBREF 6CUF 2 31 505 UNP Q2N0S6 Q2N0S6_9HIV1 30 502 DBREF 6CUF A 512 664 UNP Q2N0S7 Q2N0S7_9HIV1 509 661 DBREF 6CUF c 512 664 UNP Q2N0S7 Q2N0S7_9HIV1 509 661 DBREF 6CUF d 31 505 UNP Q2N0S6 Q2N0S6_9HIV1 30 502 SEQADV 6CUF ASN C 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 6CUF CYS C 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 6CUF CYS D 605 UNP Q2N0S7 THR 602 CONFLICT SEQADV 6CUF ASN 2 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 6CUF CYS 2 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 6CUF CYS A 605 UNP Q2N0S7 THR 602 CONFLICT SEQADV 6CUF CYS c 605 UNP Q2N0S7 THR 602 CONFLICT SEQADV 6CUF ASN d 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 6CUF CYS d 501 UNP Q2N0S6 ALA 498 CONFLICT SEQRES 1 3 211 GLN VAL GLN LEU GLN GLN SER GLY THR GLU LEU VAL TRP SEQRES 2 3 211 PRO GLY THR SER VAL THR LEU SER CYS LYS ALA SER GLY SEQRES 3 3 211 TYR THR PHE THR ASP TYR GLU ILE HIS TRP VAL LYS GLN SEQRES 4 3 211 THR PRO VAL HIS GLY LEU GLU TRP ILE GLY ALA ILE VAL SEQRES 5 3 211 PRO LYS THR GLY TYR THR ALA TYR ASN GLN LYS PHE ARG SEQRES 6 3 211 GLY LYS ALA ILE LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 3 211 ALA TYR MET ASP LEU ARG ARG LEU THR SER GLU ASP SER SEQRES 8 3 211 ALA VAL TYR TYR CYS THR ARG LEU ARG ASN TYR TRP TYR SEQRES 9 3 211 PHE ASP VAL TRP GLY THR GLY THR THR VAL THR VAL SER SEQRES 10 3 211 PRO ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 3 211 PRO GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 12 3 211 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 13 3 211 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 14 3 211 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 15 3 211 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 16 3 211 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 17 3 211 VAL GLU PRO SEQRES 1 4 219 ASP PHE LEU MET ALA GLN THR PRO LEU SER LEU PRO VAL SEQRES 2 4 219 SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER SEQRES 3 4 219 GLN SER ILE VAL TYR SER ASP GLY ASN THR TYR LEU GLU SEQRES 4 4 219 TRP TYR LEU GLN ARG PRO GLY GLN SER PRO LYS LEU LEU SEQRES 5 4 219 ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP SEQRES 6 4 219 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 4 219 ARG ILE SER ARG VAL GLU ALA GLU ASP LEU GLY ILE TYR SEQRES 8 4 219 TYR CYS PHE GLN GLY SER HIS VAL PRO TYR THR PHE GLY SEQRES 9 4 219 GLY GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 4 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 4 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 4 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 4 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 4 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 4 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 4 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 4 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 5 132 GLN VAL HIS LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 5 132 PRO SER GLU THR LEU SER LEU THR CYS ASN VAL SER GLY SEQRES 3 5 132 THR LEU VAL ARG ASP ASN TYR TRP SER TRP ILE ARG GLN SEQRES 4 5 132 PRO LEU GLY LYS GLN PRO GLU TRP ILE GLY TYR VAL HIS SEQRES 5 5 132 ASP SER GLY ASP THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 5 132 ARG VAL HIS LEU SER LEU ASP LYS SER LYS ASN LEU VAL SEQRES 7 5 132 SER LEU ARG LEU THR GLY VAL THR ALA ALA ASP SER ALA SEQRES 8 5 132 ILE TYR TYR CYS ALA THR THR LYS HIS GLY ARG ARG ILE SEQRES 9 5 132 TYR GLY VAL VAL ALA PHE LYS GLU TRP PHE THR TYR PHE SEQRES 10 5 132 TYR MET ASP VAL TRP GLY LYS GLY THR SER VAL THR VAL SEQRES 11 5 132 SER SER SEQRES 1 6 105 THR PHE VAL SER VAL ALA PRO GLY GLN THR ALA ARG ILE SEQRES 2 6 105 THR CYS GLY GLU GLU SER LEU GLY SER ARG SER VAL ILE SEQRES 3 6 105 TRP TYR GLN GLN ARG PRO GLY GLN ALA PRO SER LEU ILE SEQRES 4 6 105 ILE TYR ASN ASN ASN ASP ARG PRO SER GLY ILE PRO ASP SEQRES 5 6 105 ARG PHE SER GLY SER PRO GLY SER THR PHE GLY THR THR SEQRES 6 6 105 ALA THR LEU THR ILE THR SER VAL GLU ALA GLY ASP GLU SEQRES 7 6 105 ALA ASP TYR TYR CYS HIS ILE TRP ASP SER ARG ARG PRO SEQRES 8 6 105 THR ASN TRP VAL PHE GLY GLU GLY THR THR LEU ILE VAL SEQRES 9 6 105 LEU SEQRES 1 7 102 GLU ILE VAL LEU THR GLN SER PRO GLY ILE LEU SER LEU SEQRES 2 7 102 SER PRO GLY GLU THR ALA THR LEU PHE CYS LYS ALA SER SEQRES 3 7 102 GLN GLY GLY ASN ALA MET THR TRP TYR GLN LYS ARG ARG SEQRES 4 7 102 GLY GLN VAL PRO ARG LEU LEU ILE TYR ASP THR SER ARG SEQRES 5 7 102 ARG ALA SER GLY VAL PRO ASP ARG PHE VAL GLY SER GLY SEQRES 6 7 102 SER GLY THR ASP PHE PHE LEU THR ILE ASN LYS LEU ASP SEQRES 7 7 102 ARG GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN PHE GLU SEQRES 8 7 102 PHE PHE GLY LEU GLY SER GLU LEU GLU VAL HIS SEQRES 1 8 128 GLN VAL GLN LEU VAL GLN SER GLY ALA VAL ILE LYS THR SEQRES 2 8 128 PRO GLY SER SER VAL LYS ILE SER CYS ARG ALA SER GLY SEQRES 3 8 128 TYR ASN PHE ARG ASP TYR SER ILE HIS TRP VAL ARG LEU SEQRES 4 8 128 ILE PRO ASP LYS GLY PHE GLU TRP ILE GLY TRP ILE LYS SEQRES 5 8 128 PRO LEU TRP GLY ALA VAL SER TYR ALA ARG GLN LEU GLN SEQRES 6 8 128 GLY ARG VAL SER MET THR ARG GLN LEU SER GLN ASP PRO SEQRES 7 8 128 ASP ASP PRO ASP TRP GLY VAL ALA TYR MET GLU PHE SER SEQRES 8 8 128 GLY LEU THR PRO ALA ASP THR ALA GLU TYR PHE CYS VAL SEQRES 9 8 128 ARG ARG GLY SER CYS ASP TYR CYS GLY ASP PHE PRO TRP SEQRES 10 8 128 GLN TYR TRP GLY GLN GLY THR VAL VAL VAL VAL SEQRES 1 C 473 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 C 473 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 C 473 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 C 473 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 C 473 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 C 473 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 C 473 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 C 473 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 C 473 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 C 473 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 C 473 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 C 473 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 C 473 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 C 473 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 C 473 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 C 473 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 C 473 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 C 473 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 C 473 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 C 473 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 C 473 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 C 473 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 C 473 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 C 473 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 C 473 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 C 473 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 C 473 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 C 473 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 C 473 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 C 473 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 C 473 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 C 473 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 C 473 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 C 473 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 C 473 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 C 473 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 C 473 CYS LYS ARG ARG VAL SEQRES 1 D 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 D 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 D 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 D 153 GLN GLN SER ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 D 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 D 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 D 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 D 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 D 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 D 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 D 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 D 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 H 211 GLN VAL GLN LEU GLN GLN SER GLY THR GLU LEU VAL TRP SEQRES 2 H 211 PRO GLY THR SER VAL THR LEU SER CYS LYS ALA SER GLY SEQRES 3 H 211 TYR THR PHE THR ASP TYR GLU ILE HIS TRP VAL LYS GLN SEQRES 4 H 211 THR PRO VAL HIS GLY LEU GLU TRP ILE GLY ALA ILE VAL SEQRES 5 H 211 PRO LYS THR GLY TYR THR ALA TYR ASN GLN LYS PHE ARG SEQRES 6 H 211 GLY LYS ALA ILE LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 H 211 ALA TYR MET ASP LEU ARG ARG LEU THR SER GLU ASP SER SEQRES 8 H 211 ALA VAL TYR TYR CYS THR ARG LEU ARG ASN TYR TRP TYR SEQRES 9 H 211 PHE ASP VAL TRP GLY THR GLY THR THR VAL THR VAL SER SEQRES 10 H 211 PRO ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 H 211 PRO GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 12 H 211 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 13 H 211 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 14 H 211 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 15 H 211 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 16 H 211 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 17 H 211 VAL GLU PRO SEQRES 1 L 219 ASP PHE LEU MET ALA GLN THR PRO LEU SER LEU PRO VAL SEQRES 2 L 219 SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER SEQRES 3 L 219 GLN SER ILE VAL TYR SER ASP GLY ASN THR TYR LEU GLU SEQRES 4 L 219 TRP TYR LEU GLN ARG PRO GLY GLN SER PRO LYS LEU LEU SEQRES 5 L 219 ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP SEQRES 6 L 219 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 219 ARG ILE SER ARG VAL GLU ALA GLU ASP LEU GLY ILE TYR SEQRES 8 L 219 TYR CYS PHE GLN GLY SER HIS VAL PRO TYR THR PHE GLY SEQRES 9 L 219 GLY GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 L 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 L 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 L 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 L 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 L 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 L 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 L 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 L 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 M 132 GLN VAL HIS LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 M 132 PRO SER GLU THR LEU SER LEU THR CYS ASN VAL SER GLY SEQRES 3 M 132 THR LEU VAL ARG ASP ASN TYR TRP SER TRP ILE ARG GLN SEQRES 4 M 132 PRO LEU GLY LYS GLN PRO GLU TRP ILE GLY TYR VAL HIS SEQRES 5 M 132 ASP SER GLY ASP THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 M 132 ARG VAL HIS LEU SER LEU ASP LYS SER LYS ASN LEU VAL SEQRES 7 M 132 SER LEU ARG LEU THR GLY VAL THR ALA ALA ASP SER ALA SEQRES 8 M 132 ILE TYR TYR CYS ALA THR THR LYS HIS GLY ARG ARG ILE SEQRES 9 M 132 TYR GLY VAL VAL ALA PHE LYS GLU TRP PHE THR TYR PHE SEQRES 10 M 132 TYR MET ASP VAL TRP GLY LYS GLY THR SER VAL THR VAL SEQRES 11 M 132 SER SER SEQRES 1 N 105 THR PHE VAL SER VAL ALA PRO GLY GLN THR ALA ARG ILE SEQRES 2 N 105 THR CYS GLY GLU GLU SER LEU GLY SER ARG SER VAL ILE SEQRES 3 N 105 TRP TYR GLN GLN ARG PRO GLY GLN ALA PRO SER LEU ILE SEQRES 4 N 105 ILE TYR ASN ASN ASN ASP ARG PRO SER GLY ILE PRO ASP SEQRES 5 N 105 ARG PHE SER GLY SER PRO GLY SER THR PHE GLY THR THR SEQRES 6 N 105 ALA THR LEU THR ILE THR SER VAL GLU ALA GLY ASP GLU SEQRES 7 N 105 ALA ASP TYR TYR CYS HIS ILE TRP ASP SER ARG ARG PRO SEQRES 8 N 105 THR ASN TRP VAL PHE GLY GLU GLY THR THR LEU ILE VAL SEQRES 9 N 105 LEU SEQRES 1 Q 128 GLN VAL GLN LEU VAL GLN SER GLY ALA VAL ILE LYS THR SEQRES 2 Q 128 PRO GLY SER SER VAL LYS ILE SER CYS ARG ALA SER GLY SEQRES 3 Q 128 TYR ASN PHE ARG ASP TYR SER ILE HIS TRP VAL ARG LEU SEQRES 4 Q 128 ILE PRO ASP LYS GLY PHE GLU TRP ILE GLY TRP ILE LYS SEQRES 5 Q 128 PRO LEU TRP GLY ALA VAL SER TYR ALA ARG GLN LEU GLN SEQRES 6 Q 128 GLY ARG VAL SER MET THR ARG GLN LEU SER GLN ASP PRO SEQRES 7 Q 128 ASP ASP PRO ASP TRP GLY VAL ALA TYR MET GLU PHE SER SEQRES 8 Q 128 GLY LEU THR PRO ALA ASP THR ALA GLU TYR PHE CYS VAL SEQRES 9 Q 128 ARG ARG GLY SER CYS ASP TYR CYS GLY ASP PHE PRO TRP SEQRES 10 Q 128 GLN TYR TRP GLY GLN GLY THR VAL VAL VAL VAL SEQRES 1 R 102 GLU ILE VAL LEU THR GLN SER PRO GLY ILE LEU SER LEU SEQRES 2 R 102 SER PRO GLY GLU THR ALA THR LEU PHE CYS LYS ALA SER SEQRES 3 R 102 GLN GLY GLY ASN ALA MET THR TRP TYR GLN LYS ARG ARG SEQRES 4 R 102 GLY GLN VAL PRO ARG LEU LEU ILE TYR ASP THR SER ARG SEQRES 5 R 102 ARG ALA SER GLY VAL PRO ASP ARG PHE VAL GLY SER GLY SEQRES 6 R 102 SER GLY THR ASP PHE PHE LEU THR ILE ASN LYS LEU ASP SEQRES 7 R 102 ARG GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN PHE GLU SEQRES 8 R 102 PHE PHE GLY LEU GLY SER GLU LEU GLU VAL HIS SEQRES 1 h 211 GLN VAL GLN LEU GLN GLN SER GLY THR GLU LEU VAL TRP SEQRES 2 h 211 PRO GLY THR SER VAL THR LEU SER CYS LYS ALA SER GLY SEQRES 3 h 211 TYR THR PHE THR ASP TYR GLU ILE HIS TRP VAL LYS GLN SEQRES 4 h 211 THR PRO VAL HIS GLY LEU GLU TRP ILE GLY ALA ILE VAL SEQRES 5 h 211 PRO LYS THR GLY TYR THR ALA TYR ASN GLN LYS PHE ARG SEQRES 6 h 211 GLY LYS ALA ILE LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 h 211 ALA TYR MET ASP LEU ARG ARG LEU THR SER GLU ASP SER SEQRES 8 h 211 ALA VAL TYR TYR CYS THR ARG LEU ARG ASN TYR TRP TYR SEQRES 9 h 211 PHE ASP VAL TRP GLY THR GLY THR THR VAL THR VAL SER SEQRES 10 h 211 PRO ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 h 211 PRO GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 12 h 211 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 13 h 211 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 14 h 211 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 15 h 211 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 16 h 211 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 17 h 211 VAL GLU PRO SEQRES 1 l 219 ASP PHE LEU MET ALA GLN THR PRO LEU SER LEU PRO VAL SEQRES 2 l 219 SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER SEQRES 3 l 219 GLN SER ILE VAL TYR SER ASP GLY ASN THR TYR LEU GLU SEQRES 4 l 219 TRP TYR LEU GLN ARG PRO GLY GLN SER PRO LYS LEU LEU SEQRES 5 l 219 ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP SEQRES 6 l 219 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 l 219 ARG ILE SER ARG VAL GLU ALA GLU ASP LEU GLY ILE TYR SEQRES 8 l 219 TYR CYS PHE GLN GLY SER HIS VAL PRO TYR THR PHE GLY SEQRES 9 l 219 GLY GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA ALA SEQRES 10 l 219 PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU SEQRES 11 l 219 LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 l 219 PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP SEQRES 13 l 219 ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR SEQRES 14 l 219 GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER SEQRES 15 l 219 THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS SEQRES 16 l 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 l 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 m 132 GLN VAL HIS LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 m 132 PRO SER GLU THR LEU SER LEU THR CYS ASN VAL SER GLY SEQRES 3 m 132 THR LEU VAL ARG ASP ASN TYR TRP SER TRP ILE ARG GLN SEQRES 4 m 132 PRO LEU GLY LYS GLN PRO GLU TRP ILE GLY TYR VAL HIS SEQRES 5 m 132 ASP SER GLY ASP THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 m 132 ARG VAL HIS LEU SER LEU ASP LYS SER LYS ASN LEU VAL SEQRES 7 m 132 SER LEU ARG LEU THR GLY VAL THR ALA ALA ASP SER ALA SEQRES 8 m 132 ILE TYR TYR CYS ALA THR THR LYS HIS GLY ARG ARG ILE SEQRES 9 m 132 TYR GLY VAL VAL ALA PHE LYS GLU TRP PHE THR TYR PHE SEQRES 10 m 132 TYR MET ASP VAL TRP GLY LYS GLY THR SER VAL THR VAL SEQRES 11 m 132 SER SER SEQRES 1 n 105 THR PHE VAL SER VAL ALA PRO GLY GLN THR ALA ARG ILE SEQRES 2 n 105 THR CYS GLY GLU GLU SER LEU GLY SER ARG SER VAL ILE SEQRES 3 n 105 TRP TYR GLN GLN ARG PRO GLY GLN ALA PRO SER LEU ILE SEQRES 4 n 105 ILE TYR ASN ASN ASN ASP ARG PRO SER GLY ILE PRO ASP SEQRES 5 n 105 ARG PHE SER GLY SER PRO GLY SER THR PHE GLY THR THR SEQRES 6 n 105 ALA THR LEU THR ILE THR SER VAL GLU ALA GLY ASP GLU SEQRES 7 n 105 ALA ASP TYR TYR CYS HIS ILE TRP ASP SER ARG ARG PRO SEQRES 8 n 105 THR ASN TRP VAL PHE GLY GLU GLY THR THR LEU ILE VAL SEQRES 9 n 105 LEU SEQRES 1 q 128 GLN VAL GLN LEU VAL GLN SER GLY ALA VAL ILE LYS THR SEQRES 2 q 128 PRO GLY SER SER VAL LYS ILE SER CYS ARG ALA SER GLY SEQRES 3 q 128 TYR ASN PHE ARG ASP TYR SER ILE HIS TRP VAL ARG LEU SEQRES 4 q 128 ILE PRO ASP LYS GLY PHE GLU TRP ILE GLY TRP ILE LYS SEQRES 5 q 128 PRO LEU TRP GLY ALA VAL SER TYR ALA ARG GLN LEU GLN SEQRES 6 q 128 GLY ARG VAL SER MET THR ARG GLN LEU SER GLN ASP PRO SEQRES 7 q 128 ASP ASP PRO ASP TRP GLY VAL ALA TYR MET GLU PHE SER SEQRES 8 q 128 GLY LEU THR PRO ALA ASP THR ALA GLU TYR PHE CYS VAL SEQRES 9 q 128 ARG ARG GLY SER CYS ASP TYR CYS GLY ASP PHE PRO TRP SEQRES 10 q 128 GLN TYR TRP GLY GLN GLY THR VAL VAL VAL VAL SEQRES 1 r 102 GLU ILE VAL LEU THR GLN SER PRO GLY ILE LEU SER LEU SEQRES 2 r 102 SER PRO GLY GLU THR ALA THR LEU PHE CYS LYS ALA SER SEQRES 3 r 102 GLN GLY GLY ASN ALA MET THR TRP TYR GLN LYS ARG ARG SEQRES 4 r 102 GLY GLN VAL PRO ARG LEU LEU ILE TYR ASP THR SER ARG SEQRES 5 r 102 ARG ALA SER GLY VAL PRO ASP ARG PHE VAL GLY SER GLY SEQRES 6 r 102 SER GLY THR ASP PHE PHE LEU THR ILE ASN LYS LEU ASP SEQRES 7 r 102 ARG GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN PHE GLU SEQRES 8 r 102 PHE PHE GLY LEU GLY SER GLU LEU GLU VAL HIS SEQRES 1 2 473 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 2 473 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 2 473 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 2 473 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 2 473 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 2 473 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 2 473 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 2 473 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 2 473 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 2 473 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 2 473 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 2 473 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 2 473 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 2 473 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 2 473 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 2 473 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 2 473 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 2 473 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 2 473 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 2 473 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 2 473 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 2 473 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 2 473 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 2 473 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 2 473 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 2 473 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 2 473 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 2 473 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 2 473 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 2 473 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 2 473 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 2 473 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 2 473 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 2 473 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 2 473 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 2 473 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 2 473 CYS LYS ARG ARG VAL SEQRES 1 A 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 A 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 A 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 A 153 GLN GLN SER ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 A 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 A 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 A 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 A 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 A 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 A 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 A 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 A 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 c 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 c 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 c 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 c 153 GLN GLN SER ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 c 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 c 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 c 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 c 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 c 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 c 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 c 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 c 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 d 473 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 d 473 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 d 473 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 d 473 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 d 473 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 d 473 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 d 473 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 d 473 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 d 473 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 d 473 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 d 473 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 d 473 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 d 473 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 d 473 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 d 473 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 d 473 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 d 473 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 d 473 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 d 473 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 d 473 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 d 473 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 d 473 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 d 473 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 d 473 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 d 473 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 d 473 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 d 473 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 d 473 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 d 473 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 d 473 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 d 473 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 d 473 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 d 473 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 d 473 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 d 473 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 d 473 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 d 473 CYS LYS ARG ARG VAL HET NAG C 601 14 HET NAG C 602 14 HET NAG C 603 14 HET BMA C 604 11 HET MAN C 605 11 HET NAG C 606 14 HET NAG C 607 14 HET BMA C 608 11 HET MAN C 609 11 HET NAG C 610 14 HET NAG C 611 14 HET BMA C 612 11 HET NAG C 613 14 HET NAG C 614 14 HET NAG C 615 14 HET NAG C 616 14 HET BMA C 617 11 HET NAG C 618 14 HET NAG C 619 14 HET BMA C 620 11 HET MAN C 621 11 HET MAN C 622 11 HET MAN C 623 11 HET NAG C 624 14 HET NAG C 625 14 HET NAG C 626 14 HET NAG C 627 14 HET NAG C 628 14 HET NAG C 629 14 HET NAG C 630 14 HET BMA C 631 11 HET NAG C 632 14 HET NAG C 633 14 HET BMA C 634 11 HET MAN C 635 11 HET MAN C 636 11 HET NAG C 637 14 HET NAG C 638 14 HET NAG C 639 14 HET NAG C 640 14 HET BMA C 641 11 HET MAN C 642 11 HET MAN C 643 11 HET MAN C 644 11 HET MAN C 645 11 HET MAN C 646 11 HET MAN C 647 11 HET NAG C 648 14 HET NAG C 649 14 HET NAG C 650 14 HET NAG C 651 14 HET BMA C 652 11 HET MAN C 653 11 HET NAG D 701 14 HET NAG 2 601 14 HET NAG 2 602 14 HET NAG 2 603 14 HET BMA 2 604 11 HET MAN 2 605 11 HET NAG 2 606 14 HET NAG 2 607 14 HET BMA 2 608 11 HET MAN 2 609 11 HET NAG 2 610 14 HET NAG 2 611 14 HET BMA 2 612 11 HET NAG 2 613 14 HET NAG 2 614 14 HET NAG 2 615 14 HET NAG 2 616 14 HET BMA 2 617 11 HET NAG 2 618 14 HET NAG 2 619 14 HET BMA 2 620 11 HET MAN 2 621 11 HET MAN 2 622 11 HET MAN 2 623 11 HET NAG 2 624 14 HET NAG 2 625 14 HET NAG 2 626 14 HET NAG 2 627 14 HET NAG 2 628 14 HET NAG 2 629 14 HET NAG 2 630 14 HET BMA 2 631 11 HET NAG 2 632 14 HET NAG 2 633 14 HET BMA 2 634 11 HET MAN 2 635 11 HET MAN 2 636 11 HET NAG 2 637 14 HET NAG 2 638 14 HET NAG 2 639 14 HET NAG 2 640 14 HET BMA 2 641 11 HET MAN 2 642 11 HET MAN 2 643 11 HET MAN 2 644 11 HET MAN 2 645 11 HET MAN 2 646 11 HET MAN 2 647 11 HET NAG 2 648 14 HET NAG 2 649 14 HET NAG 2 650 14 HET NAG 2 651 14 HET BMA 2 652 11 HET MAN 2 653 11 HET NAG A 701 14 HET NAG c 701 14 HET NAG d 601 14 HET NAG d 602 14 HET NAG d 603 14 HET BMA d 604 11 HET MAN d 605 11 HET NAG d 606 14 HET NAG d 607 14 HET BMA d 608 11 HET MAN d 609 11 HET NAG d 610 14 HET NAG d 611 14 HET BMA d 612 11 HET NAG d 613 14 HET NAG d 614 14 HET NAG d 615 14 HET NAG d 616 14 HET BMA d 617 11 HET NAG d 618 14 HET NAG d 619 14 HET BMA d 620 11 HET MAN d 621 11 HET MAN d 622 11 HET MAN d 623 11 HET NAG d 624 14 HET NAG d 625 14 HET NAG d 626 14 HET NAG d 627 14 HET NAG d 628 14 HET NAG d 629 14 HET NAG d 630 14 HET BMA d 631 11 HET NAG d 632 14 HET NAG d 633 14 HET BMA d 634 11 HET MAN d 635 11 HET MAN d 636 11 HET NAG d 637 14 HET NAG d 638 14 HET NAG d 639 14 HET NAG d 640 14 HET BMA d 641 11 HET MAN d 642 11 HET MAN d 643 11 HET MAN d 644 11 HET MAN d 645 11 HET MAN d 646 11 HET MAN d 647 11 HET NAG d 648 14 HET NAG d 649 14 HET NAG d 650 14 HET NAG d 651 14 HET BMA d 652 11 HET MAN d 653 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 25 NAG 93(C8 H15 N O6) FORMUL 26 BMA 27(C6 H12 O6) FORMUL 26 MAN 42(C6 H12 O6) HELIX 1 AA1 THR 3 28 TYR 3 32 5 5 HELIX 2 AA2 THR 3 83 SER 3 87 5 5 HELIX 3 AA3 THR 5 83 SER 5 87 5 5 HELIX 4 AA4 VAL 5 100D LYS 5 100H 5 5 HELIX 5 AA5 GLU 6 79 GLU 6 83 5 5 HELIX 6 AA6 ASP 7 79 PHE 7 83 5 5 HELIX 7 AA7 ARG 8 61 GLN 8 64 5 4 HELIX 8 AA8 THR 8 83 THR 8 87 5 5 HELIX 9 AA9 ALA C 58 THR C 63 1 6 HELIX 10 AB1 VAL C 101 SER C 115 1 15 HELIX 11 AB2 THR C 123 CYS C 126 5 4 HELIX 12 AB3 TYR C 177 LEU C 179 5 3 HELIX 13 AB4 ASN C 195 THR C 198 5 4 HELIX 14 AB5 LYS C 335 ARG C 350 1 16 HELIX 15 AB6 ASP C 368 THR C 373 1 6 HELIX 16 AB7 MET C 475 SER C 481 1 7 HELIX 17 AB8 GLU C 482 TYR C 484 5 3 HELIX 18 AB9 GLY D 514 LEU D 520 1 7 HELIX 19 AC1 LEU D 523 GLY D 527 5 5 HELIX 20 AC2 THR D 529 SER D 534 1 6 HELIX 21 AC3 LEU D 537 SER D 546 1 10 HELIX 22 AC4 VAL D 570 ILE D 595 1 26 HELIX 23 AC5 ASN D 611 ASN D 616 1 6 HELIX 24 AC6 ASN D 618 MET D 626 1 9 HELIX 25 AC7 THR D 627 SER D 636 1 10 HELIX 26 AC8 GLN D 640 ASP D 664 1 25 HELIX 27 AC9 THR H 28 TYR H 32 5 5 HELIX 28 AD1 THR H 83 SER H 87 5 5 HELIX 29 AD2 THR M 83 SER M 87 5 5 HELIX 30 AD3 GLU N 79 GLU N 83 5 5 HELIX 31 AD4 ARG Q 61 GLN Q 64 5 4 HELIX 32 AD5 THR Q 83 THR Q 87 5 5 HELIX 33 AD6 ASP R 79 PHE R 83 5 5 HELIX 34 AD7 THR h 28 TYR h 32 5 5 HELIX 35 AD8 THR h 83 SER h 87 5 5 HELIX 36 AD9 THR m 83 SER m 87 5 5 HELIX 37 AE1 GLU n 79 GLU n 83 5 5 HELIX 38 AE2 ARG q 61 GLN q 64 5 4 HELIX 39 AE3 THR q 83 THR q 87 5 5 HELIX 40 AE4 ASP r 79 PHE r 83 5 5 HELIX 41 AE5 ALA 2 58 THR 2 63 1 6 HELIX 42 AE6 VAL 2 101 SER 2 115 1 15 HELIX 43 AE7 THR 2 123 CYS 2 126 5 4 HELIX 44 AE8 TYR 2 177 LEU 2 179 5 3 HELIX 45 AE9 ASN 2 195 THR 2 198 5 4 HELIX 46 AF1 LYS 2 335 ARG 2 350 1 16 HELIX 47 AF2 ASP 2 368 THR 2 373 1 6 HELIX 48 AF3 MET 2 475 SER 2 481 1 7 HELIX 49 AF4 GLU 2 482 TYR 2 484 5 3 HELIX 50 AF5 GLY A 514 LEU A 520 1 7 HELIX 51 AF6 LEU A 523 GLY A 527 5 5 HELIX 52 AF7 THR A 529 SER A 534 1 6 HELIX 53 AF8 LEU A 537 SER A 546 1 10 HELIX 54 AF9 VAL A 570 ILE A 595 1 26 HELIX 55 AG1 ASN A 611 ASN A 616 1 6 HELIX 56 AG2 ASN A 618 MET A 626 1 9 HELIX 57 AG3 THR A 627 SER A 636 1 10 HELIX 58 AG4 GLN A 640 ASP A 664 1 25 HELIX 59 AG5 GLY c 514 LEU c 520 1 7 HELIX 60 AG6 LEU c 523 GLY c 527 5 5 HELIX 61 AG7 THR c 529 SER c 534 1 6 HELIX 62 AG8 LEU c 537 SER c 546 1 10 HELIX 63 AG9 VAL c 570 ILE c 595 1 26 HELIX 64 AH1 ASN c 611 ASN c 616 1 6 HELIX 65 AH2 ASN c 618 MET c 626 1 9 HELIX 66 AH3 THR c 627 SER c 636 1 10 HELIX 67 AH4 GLN c 640 ASP c 664 1 25 HELIX 68 AH5 ALA d 58 THR d 63 1 6 HELIX 69 AH6 VAL d 101 SER d 115 1 15 HELIX 70 AH7 THR d 123 CYS d 126 5 4 HELIX 71 AH8 TYR d 177 LEU d 179 5 3 HELIX 72 AH9 ASN d 195 THR d 198 5 4 HELIX 73 AI1 LYS d 335 ARG d 350 1 16 HELIX 74 AI2 ASP d 368 THR d 373 1 6 HELIX 75 AI3 MET d 475 SER d 481 1 7 HELIX 76 AI4 GLU d 482 TYR d 484 5 3 SHEET 1 AA1 4 GLN 3 3 GLN 3 6 0 SHEET 2 AA1 4 SER 3 17 SER 3 25 -1 O LYS 3 23 N GLN 3 5 SHEET 3 AA1 4 THR 3 77 ARG 3 82A-1 O LEU 3 82 N VAL 3 18 SHEET 4 AA1 4 ALA 3 67 ASP 3 72 -1 N ILE 3 68 O ASP 3 81 SHEET 1 AA2 6 GLU 3 10 LEU 3 11 0 SHEET 2 AA2 6 THR 3 107 THR 3 110 1 O THR 3 110 N GLU 3 10 SHEET 3 AA2 6 ALA 3 88 LEU 3 95 -1 N TYR 3 90 O THR 3 107 SHEET 4 AA2 6 GLU 3 33 GLN 3 39 -1 N HIS 3 35 O THR 3 93 SHEET 5 AA2 6 GLU 3 46 ILE 3 51 -1 O ILE 3 48 N TRP 3 36 SHEET 6 AA2 6 THR 3 57 TYR 3 59 -1 O ALA 3 58 N ALA 3 50 SHEET 1 AA3 4 MET 4 4 THR 4 7 0 SHEET 2 AA3 4 ALA 4 19 SER 4 25 -1 O ARG 4 24 N ALA 4 5 SHEET 3 AA3 4 ASP 4 75 ILE 4 80 -1 O LEU 4 78 N ILE 4 21 SHEET 4 AA3 4 PHE 4 67 SER 4 72 -1 N SER 4 68 O ARG 4 79 SHEET 1 AA4 5 SER 4 10 PRO 4 12 0 SHEET 2 AA4 5 THR 4 107 GLU 4 110 1 O GLU 4 110 N LEU 4 11 SHEET 3 AA4 5 GLY 4 89 GLN 4 95 -1 N GLY 4 89 O LEU 4 109 SHEET 4 AA4 5 LEU 4 38 GLN 4 43 -1 N GLU 4 39 O PHE 4 94 SHEET 5 AA4 5 PRO 4 49 TYR 4 54 -1 O ILE 4 53 N TRP 4 40 SHEET 1 AA5 4 SER 4 10 PRO 4 12 0 SHEET 2 AA5 4 THR 4 107 GLU 4 110 1 O GLU 4 110 N LEU 4 11 SHEET 3 AA5 4 GLY 4 89 GLN 4 95 -1 N GLY 4 89 O LEU 4 109 SHEET 4 AA5 4 THR 4 102 PHE 4 103 -1 O THR 4 102 N GLN 4 95 SHEET 1 AA6 4 GLN 5 5 SER 5 7 0 SHEET 2 AA6 4 SER 5 19 ASN 5 23 -1 O ASN 5 23 N GLN 5 5 SHEET 3 AA6 4 LEU 5 77 LEU 5 82 -1 O LEU 5 80 N LEU 5 20 SHEET 4 AA6 4 VAL 5 67 ASP 5 72 -1 N HIS 5 68 O ARG 5 81 SHEET 1 AA7 2 LEU 5 11 VAL 5 12 0 SHEET 2 AA7 2 THR 5 108 VAL 5 109 1 O THR 5 108 N VAL 5 12 SHEET 1 AA8 4 GLU 5 46 VAL 5 51 0 SHEET 2 AA8 4 TRP 5 34 GLN 5 39 -1 N TRP 5 34 O VAL 5 51 SHEET 3 AA8 4 ILE 5 89 ALA 5 93 -1 O ILE 5 89 N GLN 5 39 SHEET 4 AA8 4 THR 5 105 SER 5 106 -1 O THR 5 105 N TYR 5 90 SHEET 1 AA9 2 LYS 5 96 ILE 5 100A 0 SHEET 2 AA9 2 TRP 5 100J TYR 5 100O-1 O PHE 5 100K N ARG 5 100 SHEET 1 AB1 5 PHE 6 9 VAL 6 13 0 SHEET 2 AB1 5 THR 6 102 VAL 6 106 1 O ILE 6 105 N VAL 6 11 SHEET 3 AB1 5 ASP 6 85 HIS 6 89 -1 N TYR 6 86 O THR 6 102 SHEET 4 AB1 5 ILE 6 34 GLN 6 38 -1 N GLN 6 38 O ASP 6 85 SHEET 5 AB1 5 PRO 6 44 ILE 6 48 -1 O ILE 6 48 N TRP 6 35 SHEET 1 AB2 3 ALA 6 19 GLU 6 26 0 SHEET 2 AB2 3 THR 6 70 ILE 6 75 -1 O ILE 6 75 N ALA 6 19 SHEET 3 AB2 3 PHE 6 62 GLY 6 64 -1 N SER 6 63 O THR 6 74 SHEET 1 AB3 4 LEU 7 4 GLN 7 6 0 SHEET 2 AB3 4 ALA 7 19 ALA 7 25 -1 O LYS 7 24 N THR 7 5 SHEET 3 AB3 4 ASP 7 70 ILE 7 75 -1 O LEU 7 73 N LEU 7 21 SHEET 4 AB3 4 PHE 7 62 SER 7 67 -1 N VAL 7 63 O THR 7 74 SHEET 1 AB4 6 ILE 7 10 LEU 7 13 0 SHEET 2 AB4 6 SER 7 102 VAL 7 106 1 O GLU 7 105 N LEU 7 13 SHEET 3 AB4 6 VAL 7 85 GLN 7 89 -1 N TYR 7 86 O SER 7 102 SHEET 4 AB4 6 THR 7 34 LYS 7 38 -1 N LYS 7 38 O VAL 7 85 SHEET 5 AB4 6 ARG 7 45 TYR 7 49 -1 O ILE 7 48 N TRP 7 35 SHEET 6 AB4 6 ARG 7 53 ARG 7 54 -1 O ARG 7 53 N TYR 7 49 SHEET 1 AB5 4 GLN 8 3 GLN 8 6 0 SHEET 2 AB5 4 SER 8 17 SER 8 25 -1 O SER 8 25 N GLN 8 3 SHEET 3 AB5 4 GLY 8 76G SER 8 82A-1 O GLY 8 76G N ALA 8 24 SHEET 4 AB5 4 VAL 8 67 SER 8 68 -1 N SER 8 68 O GLU 8 81 SHEET 1 AB6 4 GLN 8 3 GLN 8 6 0 SHEET 2 AB6 4 SER 8 17 SER 8 25 -1 O SER 8 25 N GLN 8 3 SHEET 3 AB6 4 GLY 8 76G SER 8 82A-1 O GLY 8 76G N ALA 8 24 SHEET 4 AB6 4 ARG 8 71 GLN 8 72 -1 N GLN 8 72 O VAL 8 77 SHEET 1 AB7 6 VAL 8 10 ILE 8 11 0 SHEET 2 AB7 6 THR 8 107 VAL 8 110 1 O VAL 8 110 N VAL 8 10 SHEET 3 AB7 6 ALA 8 88 ARG 8 95 -1 N ALA 8 88 O VAL 8 109 SHEET 4 AB7 6 ILE 8 34 ILE 8 40 -1 N LEU 8 39 O GLU 8 89 SHEET 5 AB7 6 GLY 8 44 LYS 8 52 -1 O GLY 8 49 N TRP 8 36 SHEET 6 AB7 6 ALA 8 56 TYR 8 59 -1 O SER 8 58 N TRP 8 50 SHEET 1 AB8 4 VAL 8 10 ILE 8 11 0 SHEET 2 AB8 4 THR 8 107 VAL 8 110 1 O VAL 8 110 N VAL 8 10 SHEET 3 AB8 4 ALA 8 88 ARG 8 95 -1 N ALA 8 88 O VAL 8 109 SHEET 4 AB8 4 TRP 8 100F TYR 8 102 -1 O TYR 8 102 N ARG 8 94 SHEET 1 AB9 2 TRP C 35 TYR C 39 0 SHEET 2 AB9 2 GLY C 495 THR C 499 -1 O THR C 499 N TRP C 35 SHEET 1 AC1 4 TRP C 45 ASP C 47 0 SHEET 2 AC1 4 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AC1 4 PHE C 223 CYS C 228 -1 N ALA C 224 O VAL C 489 SHEET 4 AC1 4 VAL C 242 VAL C 245 -1 O VAL C 245 N ILE C 225 SHEET 1 AC2 3 VAL C 75 PRO C 76 0 SHEET 2 AC2 3 PHE C 53 SER C 56 1 N SER C 56 O VAL C 75 SHEET 3 AC2 3 HIS C 216 CYS C 218 -1 O HIS C 216 N ALA C 55 SHEET 1 AC3 2 GLU C 91 ASN C 94 0 SHEET 2 AC3 2 THR C 236 CYS C 239 -1 O GLY C 237 N PHE C 93 SHEET 1 AC4 2 VAL C 120 LYS C 121 0 SHEET 2 AC4 2 THR C 202 GLN C 203 -1 O GLN C 203 N VAL C 120 SHEET 1 AC5 3 GLN C 130 ASN C 133 0 SHEET 2 AC5 3 LYS C 155 THR C 162 -1 O SER C 158 N GLN C 130 SHEET 3 AC5 3 LYS C 169 PHE C 176 -1 O SER C 174 N CYS C 157 SHEET 1 AC6 2 VAL C 181 ILE C 184 0 SHEET 2 AC6 2 GLU C 190 LEU C 193 -1 O GLU C 190 N ILE C 184 SHEET 1 AC7 6 MET C 271 ARG C 273 0 SHEET 2 AC7 6 ILE C 284 ASN C 302 -1 O LEU C 285 N ARG C 273 SHEET 3 AC7 6 HIS C 330 SER C 334 -1 O HIS C 330 N THR C 297 SHEET 4 AC7 6 SER C 413 ARG C 419 -1 O ILE C 414 N VAL C 333 SHEET 5 AC7 6 PHE C 382 CYS C 385 -1 N TYR C 384 O ARG C 419 SHEET 6 AC7 6 HIS C 374 ASN C 377 -1 N PHE C 376 O PHE C 383 SHEET 1 AC8 4 MET C 271 ARG C 273 0 SHEET 2 AC8 4 ILE C 284 ASN C 302 -1 O LEU C 285 N ARG C 273 SHEET 3 AC8 4 GLY C 441 ARG C 456 -1 O LEU C 454 N ILE C 284 SHEET 4 AC8 4 PHE C 468 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 1 AC9 2 ARG C 304 SER C 306 0 SHEET 2 AC9 2 TYR C 318 THR C 320 -1 O ALA C 319 N LYS C 305 SHEET 1 AD1 2 ILE C 359 ARG C 360 0 SHEET 2 AD1 2 THR C 394 TRP C 395 -1 O TRP C 395 N ILE C 359 SHEET 1 AD2 4 GLN H 3 GLN H 6 0 SHEET 2 AD2 4 SER H 17 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AD2 4 THR H 77 ARG H 82A-1 O LEU H 82 N VAL H 18 SHEET 4 AD2 4 ALA H 67 ASP H 72 -1 N ILE H 68 O ASP H 81 SHEET 1 AD3 6 GLU H 10 LEU H 11 0 SHEET 2 AD3 6 THR H 107 THR H 110 1 O THR H 110 N GLU H 10 SHEET 3 AD3 6 ALA H 88 LEU H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AD3 6 GLU H 33 THR H 40 -1 N HIS H 35 O THR H 93 SHEET 5 AD3 6 GLY H 44 ILE H 51 -1 O ILE H 48 N TRP H 36 SHEET 6 AD3 6 THR H 57 TYR H 59 -1 O ALA H 58 N ALA H 50 SHEET 1 AD4 4 MET L 4 THR L 7 0 SHEET 2 AD4 4 ALA L 19 SER L 25 -1 O ARG L 24 N ALA L 5 SHEET 3 AD4 4 ASP L 75 ILE L 80 -1 O LEU L 78 N ILE L 21 SHEET 4 AD4 4 PHE L 67 SER L 72 -1 N SER L 70 O THR L 77 SHEET 1 AD5 5 SER L 10 PRO L 12 0 SHEET 2 AD5 5 THR L 107 GLU L 110 1 O GLU L 110 N LEU L 11 SHEET 3 AD5 5 GLY L 89 GLN L 95 -1 N TYR L 91 O THR L 107 SHEET 4 AD5 5 LEU L 38 GLN L 43 -1 N GLN L 43 O ILE L 90 SHEET 5 AD5 5 PRO L 49 TYR L 54 -1 O ILE L 53 N TRP L 40 SHEET 1 AD6 4 SER L 10 PRO L 12 0 SHEET 2 AD6 4 THR L 107 GLU L 110 1 O GLU L 110 N LEU L 11 SHEET 3 AD6 4 GLY L 89 GLN L 95 -1 N TYR L 91 O THR L 107 SHEET 4 AD6 4 THR L 102 PHE L 103 -1 O THR L 102 N GLN L 95 SHEET 1 AD7 4 GLN M 5 SER M 7 0 SHEET 2 AD7 4 SER M 19 ASN M 23 -1 O ASN M 23 N GLN M 5 SHEET 3 AD7 4 LEU M 77 LEU M 82 -1 O LEU M 80 N LEU M 20 SHEET 4 AD7 4 VAL M 67 ASP M 72 -1 N HIS M 68 O ARG M 81 SHEET 1 AD8 2 LEU M 11 VAL M 12 0 SHEET 2 AD8 2 THR M 108 VAL M 109 1 O THR M 108 N VAL M 12 SHEET 1 AD9 4 GLU M 46 VAL M 51 0 SHEET 2 AD9 4 TYR M 33 GLN M 39 -1 N TRP M 34 O VAL M 51 SHEET 3 AD9 4 ILE M 89 ILE M 100A-1 O TYR M 91 N ILE M 37 SHEET 4 AD9 4 TRP M 100J TYR M 100O-1 O TYR M 100O N LYS M 96 SHEET 1 AE1 5 PHE N 9 VAL N 13 0 SHEET 2 AE1 5 THR N 102 VAL N 106 1 O ILE N 105 N VAL N 11 SHEET 3 AE1 5 ASP N 85 HIS N 89 -1 N TYR N 86 O THR N 102 SHEET 4 AE1 5 ILE N 34 GLN N 38 -1 N GLN N 38 O ASP N 85 SHEET 5 AE1 5 PRO N 44 ILE N 48 -1 O ILE N 48 N TRP N 35 SHEET 1 AE2 3 ALA N 19 GLU N 26 0 SHEET 2 AE2 3 THR N 70 ILE N 75 -1 O ILE N 75 N ALA N 19 SHEET 3 AE2 3 PHE N 62 GLY N 64 -1 N SER N 63 O THR N 74 SHEET 1 AE3 4 GLN Q 3 GLN Q 6 0 SHEET 2 AE3 4 SER Q 17 SER Q 25 -1 O ARG Q 23 N VAL Q 5 SHEET 3 AE3 4 GLY Q 76G SER Q 82A-1 O ALA Q 78 N CYS Q 22 SHEET 4 AE3 4 VAL Q 67 SER Q 68 -1 N SER Q 68 O GLU Q 81 SHEET 1 AE4 4 GLN Q 3 GLN Q 6 0 SHEET 2 AE4 4 SER Q 17 SER Q 25 -1 O ARG Q 23 N VAL Q 5 SHEET 3 AE4 4 GLY Q 76G SER Q 82A-1 O ALA Q 78 N CYS Q 22 SHEET 4 AE4 4 ARG Q 71 GLN Q 72 -1 N GLN Q 72 O VAL Q 77 SHEET 1 AE5 6 VAL Q 10 ILE Q 11 0 SHEET 2 AE5 6 THR Q 107 VAL Q 110 1 O VAL Q 110 N VAL Q 10 SHEET 3 AE5 6 ALA Q 88 ARG Q 95 -1 N ALA Q 88 O VAL Q 109 SHEET 4 AE5 6 ILE Q 34 ILE Q 40 -1 N HIS Q 35 O VAL Q 93 SHEET 5 AE5 6 GLY Q 44 LYS Q 52 -1 O GLY Q 49 N TRP Q 36 SHEET 6 AE5 6 ALA Q 56 TYR Q 59 -1 O SER Q 58 N TRP Q 50 SHEET 1 AE6 4 VAL Q 10 ILE Q 11 0 SHEET 2 AE6 4 THR Q 107 VAL Q 110 1 O VAL Q 110 N VAL Q 10 SHEET 3 AE6 4 ALA Q 88 ARG Q 95 -1 N ALA Q 88 O VAL Q 109 SHEET 4 AE6 4 TRP Q 100F TRP Q 103 -1 O TYR Q 102 N ARG Q 94 SHEET 1 AE7 4 LEU R 4 GLN R 6 0 SHEET 2 AE7 4 ALA R 19 ALA R 25 -1 O LYS R 24 N THR R 5 SHEET 3 AE7 4 ASP R 70 ILE R 75 -1 O LEU R 73 N LEU R 21 SHEET 4 AE7 4 PHE R 62 SER R 67 -1 N VAL R 63 O THR R 74 SHEET 1 AE8 6 ILE R 10 LEU R 13 0 SHEET 2 AE8 6 SER R 102 VAL R 106 1 O GLU R 105 N LEU R 13 SHEET 3 AE8 6 VAL R 85 GLN R 89 -1 N TYR R 86 O SER R 102 SHEET 4 AE8 6 THR R 34 LYS R 38 -1 N LYS R 38 O VAL R 85 SHEET 5 AE8 6 ARG R 45 TYR R 49 -1 O ARG R 45 N GLN R 37 SHEET 6 AE8 6 ARG R 53 ARG R 54 -1 O ARG R 53 N TYR R 49 SHEET 1 AE9 4 GLN h 3 GLN h 6 0 SHEET 2 AE9 4 SER h 17 SER h 25 -1 O LYS h 23 N GLN h 5 SHEET 3 AE9 4 THR h 77 ARG h 82A-1 O LEU h 82 N VAL h 18 SHEET 4 AE9 4 ALA h 67 ASP h 72 -1 N ILE h 68 O ASP h 81 SHEET 1 AF1 6 GLU h 10 LEU h 11 0 SHEET 2 AF1 6 THR h 107 THR h 110 1 O THR h 108 N GLU h 10 SHEET 3 AF1 6 ALA h 88 ARG h 94 -1 N TYR h 90 O THR h 107 SHEET 4 AF1 6 ILE h 34 THR h 40 -1 N HIS h 35 O THR h 93 SHEET 5 AF1 6 GLY h 44 ILE h 51 -1 O ILE h 48 N TRP h 36 SHEET 6 AF1 6 THR h 57 TYR h 59 -1 O ALA h 58 N ALA h 50 SHEET 1 AF2 4 MET l 4 THR l 7 0 SHEET 2 AF2 4 ALA l 19 SER l 25 -1 O ARG l 24 N ALA l 5 SHEET 3 AF2 4 ASP l 75 ILE l 80 -1 O LEU l 78 N ILE l 21 SHEET 4 AF2 4 PHE l 67 SER l 72 -1 N SER l 68 O ARG l 79 SHEET 1 AF3 5 SER l 10 PRO l 12 0 SHEET 2 AF3 5 THR l 107 GLU l 110 1 O GLU l 110 N LEU l 11 SHEET 3 AF3 5 GLY l 89 GLN l 95 -1 N TYR l 91 O THR l 107 SHEET 4 AF3 5 LEU l 38 GLN l 43 -1 N GLU l 39 O PHE l 94 SHEET 5 AF3 5 PRO l 49 TYR l 54 -1 O ILE l 53 N TRP l 40 SHEET 1 AF4 4 SER l 10 PRO l 12 0 SHEET 2 AF4 4 THR l 107 GLU l 110 1 O GLU l 110 N LEU l 11 SHEET 3 AF4 4 GLY l 89 GLN l 95 -1 N TYR l 91 O THR l 107 SHEET 4 AF4 4 THR l 102 PHE l 103 -1 O THR l 102 N GLN l 95 SHEET 1 AF5 4 GLN m 5 SER m 7 0 SHEET 2 AF5 4 SER m 19 ASN m 23 -1 O THR m 21 N SER m 7 SHEET 3 AF5 4 LEU m 77 LEU m 82 -1 O LEU m 80 N LEU m 20 SHEET 4 AF5 4 VAL m 67 ASP m 72 -1 N HIS m 68 O ARG m 81 SHEET 1 AF6 5 LEU m 11 VAL m 12 0 SHEET 2 AF6 5 SER m 106 VAL m 109 1 O THR m 108 N VAL m 12 SHEET 3 AF6 5 ALA m 88 ILE m 100A-1 N ALA m 88 O VAL m 107 SHEET 4 AF6 5 TYR m 33 GLN m 39 -1 N GLN m 39 O ILE m 89 SHEET 5 AF6 5 GLU m 46 VAL m 51 -1 O VAL m 51 N TRP m 34 SHEET 1 AF7 4 LEU m 11 VAL m 12 0 SHEET 2 AF7 4 SER m 106 VAL m 109 1 O THR m 108 N VAL m 12 SHEET 3 AF7 4 ALA m 88 ILE m 100A-1 N ALA m 88 O VAL m 107 SHEET 4 AF7 4 TRP m 100J TYR m 100O-1 O PHE m 100K N ARG m 100 SHEET 1 AF8 5 PHE n 9 VAL n 13 0 SHEET 2 AF8 5 THR n 102 VAL n 106 1 O ILE n 105 N VAL n 11 SHEET 3 AF8 5 ASP n 85 HIS n 89 -1 N TYR n 86 O THR n 102 SHEET 4 AF8 5 ILE n 34 GLN n 38 -1 N GLN n 38 O ASP n 85 SHEET 5 AF8 5 PRO n 44 ILE n 48 -1 O ILE n 48 N TRP n 35 SHEET 1 AF9 3 ALA n 19 GLU n 26 0 SHEET 2 AF9 3 THR n 70 ILE n 75 -1 O ILE n 75 N ALA n 19 SHEET 3 AF9 3 PHE n 62 GLY n 64 -1 N SER n 63 O THR n 74 SHEET 1 AG1 4 GLN q 3 VAL q 5 0 SHEET 2 AG1 4 SER q 17 SER q 25 -1 O ARG q 23 N VAL q 5 SHEET 3 AG1 4 GLY q 76G SER q 82A-1 O GLY q 76G N ALA q 24 SHEET 4 AG1 4 VAL q 67 SER q 68 -1 N SER q 68 O GLU q 81 SHEET 1 AG2 4 GLN q 3 VAL q 5 0 SHEET 2 AG2 4 SER q 17 SER q 25 -1 O ARG q 23 N VAL q 5 SHEET 3 AG2 4 GLY q 76G SER q 82A-1 O GLY q 76G N ALA q 24 SHEET 4 AG2 4 ARG q 71 GLN q 72 -1 N GLN q 72 O VAL q 77 SHEET 1 AG3 6 VAL q 10 ILE q 11 0 SHEET 2 AG3 6 THR q 107 VAL q 110 1 O VAL q 110 N VAL q 10 SHEET 3 AG3 6 ALA q 88 ARG q 95 -1 N TYR q 90 O THR q 107 SHEET 4 AG3 6 ILE q 34 ILE q 40 -1 N HIS q 35 O VAL q 93 SHEET 5 AG3 6 GLY q 44 LYS q 52 -1 O GLY q 49 N TRP q 36 SHEET 6 AG3 6 ALA q 56 TYR q 59 -1 O SER q 58 N TRP q 50 SHEET 1 AG4 4 VAL q 10 ILE q 11 0 SHEET 2 AG4 4 THR q 107 VAL q 110 1 O VAL q 110 N VAL q 10 SHEET 3 AG4 4 ALA q 88 ARG q 95 -1 N TYR q 90 O THR q 107 SHEET 4 AG4 4 TRP q 100F TRP q 103 -1 O TYR q 102 N ARG q 94 SHEET 1 AG5 4 THR r 5 GLN r 6 0 SHEET 2 AG5 4 ALA r 19 LYS r 24 -1 O LYS r 24 N THR r 5 SHEET 3 AG5 4 ASP r 70 ILE r 75 -1 O LEU r 73 N LEU r 21 SHEET 4 AG5 4 PHE r 62 SER r 67 -1 N VAL r 63 O THR r 74 SHEET 1 AG6 6 ILE r 10 LEU r 13 0 SHEET 2 AG6 6 SER r 102 VAL r 106 1 O GLU r 103 N LEU r 11 SHEET 3 AG6 6 VAL r 85 GLN r 89 -1 N TYR r 86 O SER r 102 SHEET 4 AG6 6 THR r 34 LYS r 38 -1 N LYS r 38 O VAL r 85 SHEET 5 AG6 6 ARG r 45 TYR r 49 -1 O ARG r 45 N GLN r 37 SHEET 6 AG6 6 ARG r 53 ARG r 54 -1 O ARG r 53 N TYR r 49 SHEET 1 AG7 2 TRP 2 35 TYR 2 39 0 SHEET 2 AG7 2 GLY 2 495 THR 2 499 -1 O THR 2 499 N TRP 2 35 SHEET 1 AG8 4 TRP 2 45 ASP 2 47 0 SHEET 2 AG8 4 TYR 2 486 ILE 2 491 -1 O LYS 2 490 N LYS 2 46 SHEET 3 AG8 4 PHE 2 223 CYS 2 228 -1 N ALA 2 224 O VAL 2 489 SHEET 4 AG8 4 VAL 2 242 VAL 2 245 -1 O VAL 2 245 N ILE 2 225 SHEET 1 AG9 3 VAL 2 75 PRO 2 76 0 SHEET 2 AG9 3 PHE 2 53 SER 2 56 1 N SER 2 56 O VAL 2 75 SHEET 3 AG9 3 HIS 2 216 CYS 2 218 -1 O HIS 2 216 N ALA 2 55 SHEET 1 AH1 2 GLU 2 91 ASN 2 94 0 SHEET 2 AH1 2 THR 2 236 CYS 2 239 -1 O GLY 2 237 N PHE 2 93 SHEET 1 AH2 2 VAL 2 120 LYS 2 121 0 SHEET 2 AH2 2 THR 2 202 GLN 2 203 -1 O GLN 2 203 N VAL 2 120 SHEET 1 AH3 3 GLN 2 130 ASN 2 133 0 SHEET 2 AH3 3 LYS 2 155 THR 2 162 -1 O SER 2 158 N GLN 2 130 SHEET 3 AH3 3 LYS 2 169 PHE 2 176 -1 O SER 2 174 N CYS 2 157 SHEET 1 AH4 2 VAL 2 181 ILE 2 184 0 SHEET 2 AH4 2 GLU 2 190 LEU 2 193 -1 O GLU 2 190 N ILE 2 184 SHEET 1 AH5 6 MET 2 271 ARG 2 273 0 SHEET 2 AH5 6 ILE 2 284 ASN 2 302 -1 O LEU 2 285 N ARG 2 273 SHEET 3 AH5 6 HIS 2 330 SER 2 334 -1 O HIS 2 330 N THR 2 297 SHEET 4 AH5 6 SER 2 413 ARG 2 419 -1 O ILE 2 414 N VAL 2 333 SHEET 5 AH5 6 PHE 2 382 CYS 2 385 -1 N TYR 2 384 O ARG 2 419 SHEET 6 AH5 6 HIS 2 374 ASN 2 377 -1 N PHE 2 376 O PHE 2 383 SHEET 1 AH6 4 MET 2 271 ARG 2 273 0 SHEET 2 AH6 4 ILE 2 284 ASN 2 302 -1 O LEU 2 285 N ARG 2 273 SHEET 3 AH6 4 GLY 2 441 ARG 2 456 -1 O LEU 2 454 N ILE 2 284 SHEET 4 AH6 4 PHE 2 468 PRO 2 470 -1 O ARG 2 469 N THR 2 455 SHEET 1 AH7 2 ARG 2 304 SER 2 306 0 SHEET 2 AH7 2 TYR 2 318 THR 2 320 -1 O ALA 2 319 N LYS 2 305 SHEET 1 AH8 2 ILE 2 359 ARG 2 360 0 SHEET 2 AH8 2 THR 2 394 TRP 2 395 -1 O TRP 2 395 N ILE 2 359 SHEET 1 AH9 2 TRP d 35 TYR d 39 0 SHEET 2 AH9 2 GLY d 495 THR d 499 -1 O THR d 499 N TRP d 35 SHEET 1 AI1 4 TRP d 45 ASP d 47 0 SHEET 2 AI1 4 TYR d 486 ILE d 491 -1 O LYS d 490 N LYS d 46 SHEET 3 AI1 4 PHE d 223 CYS d 228 -1 N ALA d 224 O VAL d 489 SHEET 4 AI1 4 VAL d 242 VAL d 245 -1 O VAL d 245 N ILE d 225 SHEET 1 AI2 3 VAL d 75 PRO d 76 0 SHEET 2 AI2 3 PHE d 53 SER d 56 1 N SER d 56 O VAL d 75 SHEET 3 AI2 3 HIS d 216 CYS d 218 -1 O HIS d 216 N ALA d 55 SHEET 1 AI3 2 GLU d 91 ASN d 94 0 SHEET 2 AI3 2 THR d 236 CYS d 239 -1 O GLY d 237 N PHE d 93 SHEET 1 AI4 2 VAL d 120 LYS d 121 0 SHEET 2 AI4 2 THR d 202 GLN d 203 -1 O GLN d 203 N VAL d 120 SHEET 1 AI5 3 GLN d 130 ASN d 133 0 SHEET 2 AI5 3 LYS d 155 THR d 162 -1 O SER d 158 N GLN d 130 SHEET 3 AI5 3 LYS d 169 PHE d 176 -1 O SER d 174 N CYS d 157 SHEET 1 AI6 2 VAL d 181 ILE d 184 0 SHEET 2 AI6 2 GLU d 190 LEU d 193 -1 O GLU d 190 N ILE d 184 SHEET 1 AI7 6 MET d 271 ARG d 273 0 SHEET 2 AI7 6 ILE d 284 ASN d 302 -1 O LEU d 285 N ARG d 273 SHEET 3 AI7 6 HIS d 330 SER d 334 -1 O HIS d 330 N THR d 297 SHEET 4 AI7 6 SER d 413 ARG d 419 -1 O ILE d 414 N VAL d 333 SHEET 5 AI7 6 PHE d 382 CYS d 385 -1 N TYR d 384 O ARG d 419 SHEET 6 AI7 6 HIS d 374 ASN d 377 -1 N PHE d 376 O PHE d 383 SHEET 1 AI8 4 MET d 271 ARG d 273 0 SHEET 2 AI8 4 ILE d 284 ASN d 302 -1 O LEU d 285 N ARG d 273 SHEET 3 AI8 4 GLY d 441 ARG d 456 -1 O LEU d 454 N ILE d 284 SHEET 4 AI8 4 PHE d 468 PRO d 470 -1 O ARG d 469 N THR d 455 SHEET 1 AI9 2 ARG d 304 SER d 306 0 SHEET 2 AI9 2 TYR d 318 THR d 320 -1 O ALA d 319 N LYS d 305 SHEET 1 AJ1 2 ILE d 359 ARG d 360 0 SHEET 2 AJ1 2 THR d 394 TRP d 395 -1 O TRP d 395 N ILE d 359 SSBOND 1 CYS 3 22 CYS 3 92 1555 1555 2.03 SSBOND 2 CYS 4 23 CYS 4 93 1555 1555 2.04 SSBOND 3 CYS 5 22 CYS 5 92 1555 1555 2.04 SSBOND 4 CYS 6 23 CYS 6 88 1555 1555 2.03 SSBOND 5 CYS 8 22 CYS 8 92 1555 1555 2.04 SSBOND 6 CYS 8 98 CYS 8 100A 1555 1555 2.03 SSBOND 7 CYS C 119 CYS C 205 1555 1555 2.02 SSBOND 8 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 9 CYS C 131 CYS C 157 1555 1555 2.04 SSBOND 10 CYS C 218 CYS C 247 1555 1555 2.03 SSBOND 11 CYS C 228 CYS C 239 1555 1555 2.04 SSBOND 12 CYS C 296 CYS C 331 1555 1555 2.02 SSBOND 13 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 14 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 15 CYS D 598 CYS D 604 1555 1555 2.02 SSBOND 16 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 17 CYS L 23 CYS L 93 1555 1555 2.04 SSBOND 18 CYS M 22 CYS M 92 1555 1555 2.04 SSBOND 19 CYS N 23 CYS N 88 1555 1555 2.03 SSBOND 20 CYS Q 22 CYS Q 92 1555 1555 2.04 SSBOND 21 CYS Q 98 CYS Q 100A 1555 1555 2.03 SSBOND 22 CYS h 22 CYS h 92 1555 1555 2.03 SSBOND 23 CYS l 23 CYS l 93 1555 1555 2.04 SSBOND 24 CYS m 22 CYS m 92 1555 1555 2.03 SSBOND 25 CYS n 23 CYS n 88 1555 1555 2.03 SSBOND 26 CYS q 22 CYS q 92 1555 1555 2.04 SSBOND 27 CYS q 98 CYS q 100A 1555 1555 2.03 SSBOND 28 CYS 2 119 CYS 2 205 1555 1555 2.02 SSBOND 29 CYS 2 126 CYS 2 196 1555 1555 2.03 SSBOND 30 CYS 2 131 CYS 2 157 1555 1555 2.04 SSBOND 31 CYS 2 218 CYS 2 247 1555 1555 2.03 SSBOND 32 CYS 2 228 CYS 2 239 1555 1555 2.04 SSBOND 33 CYS 2 296 CYS 2 331 1555 1555 2.02 SSBOND 34 CYS 2 378 CYS 2 445 1555 1555 2.03 SSBOND 35 CYS 2 385 CYS 2 418 1555 1555 2.03 SSBOND 36 CYS A 598 CYS A 604 1555 1555 2.02 SSBOND 37 CYS c 598 CYS c 604 1555 1555 2.02 SSBOND 38 CYS d 119 CYS d 205 1555 1555 2.03 SSBOND 39 CYS d 126 CYS d 196 1555 1555 2.03 SSBOND 40 CYS d 131 CYS d 157 1555 1555 2.04 SSBOND 41 CYS d 218 CYS d 247 1555 1555 2.03 SSBOND 42 CYS d 228 CYS d 239 1555 1555 2.04 SSBOND 43 CYS d 296 CYS d 331 1555 1555 2.02 SSBOND 44 CYS d 378 CYS d 445 1555 1555 2.03 SSBOND 45 CYS d 385 CYS d 418 1555 1555 2.03 LINK ND2 ASN C 133 C1 NAG C 601 1555 1555 1.39 LINK ND2 ASN C 133 C2 NAG C 601 1555 1555 1.60 LINK ND2 ASN C 137 C1 NAG C 602 1555 1555 1.52 LINK ND2 ASN C 156 C1 NAG C 606 1555 1555 1.31 LINK ND2 ASN C 160 C1 NAG C 610 1555 1555 1.39 LINK ND2 ASN C 197 C1 NAG C 613 1555 1555 1.49 LINK ND2 ASN C 234 C1 NAG C 615 1555 1555 1.41 LINK ND2 ASN C 234 O5 NAG C 615 1555 1555 1.42 LINK ND2 ASN C 262 C1 NAG C 618 1555 1555 1.42 LINK ND2 ASN C 276 C1 NAG C 650 1555 1555 1.39 LINK ND2 ASN C 301 C1 NAG C 626 1555 1555 1.40 LINK ND2 ASN C 332 C1 NAG C 639 1555 1555 1.43 LINK ND2 ASN C 355 C1 NAG C 628 1555 1555 1.40 LINK ND2 ASN C 363 C1 NAG C 629 1555 1555 1.36 LINK ND2 ASN C 386 C1 NAG C 632 1555 1555 1.37 LINK ND2 ASN C 392 C1 NAG C 637 1555 1555 1.42 LINK ND2 ASN C 448 C1 NAG C 648 1555 1555 1.35 LINK ND2 ASN D 637 C1 NAG D 701 1555 1555 1.38 LINK ND2 ASN 2 133 C1 NAG 2 601 1555 1555 1.39 LINK ND2 ASN 2 133 C2 NAG 2 601 1555 1555 1.60 LINK ND2 ASN 2 137 C1 NAG 2 602 1555 1555 1.52 LINK ND2 ASN 2 156 C1 NAG 2 606 1555 1555 1.38 LINK ND2 ASN 2 156 O5 NAG 2 606 1555 1555 1.36 LINK ND2 ASN 2 160 C1 NAG 2 610 1555 1555 1.39 LINK ND2 ASN 2 197 C1 NAG 2 613 1555 1555 1.49 LINK ND2 ASN 2 234 C1 NAG 2 615 1555 1555 1.41 LINK ND2 ASN 2 234 O5 NAG 2 615 1555 1555 1.42 LINK ND2 ASN 2 262 C1 NAG 2 618 1555 1555 1.42 LINK ND2 ASN 2 276 C1 NAG 2 650 1555 1555 1.39 LINK ND2 ASN 2 301 C1 NAG 2 626 1555 1555 1.40 LINK ND2 ASN 2 332 C1 NAG 2 639 1555 1555 1.43 LINK ND2 ASN 2 355 C1 NAG 2 628 1555 1555 1.40 LINK ND2 ASN 2 363 C1 NAG 2 629 1555 1555 1.36 LINK ND2 ASN 2 386 C1 NAG 2 632 1555 1555 1.37 LINK ND2 ASN 2 392 C1 NAG 2 637 1555 1555 1.42 LINK ND2 ASN 2 448 C1 NAG 2 648 1555 1555 1.35 LINK ND2 ASN A 637 C1 NAG A 701 1555 1555 1.38 LINK ND2 ASN c 637 C1 NAG c 701 1555 1555 1.37 LINK ND2 ASN d 133 C1 NAG d 601 1555 1555 1.39 LINK ND2 ASN d 133 C2 NAG d 601 1555 1555 1.60 LINK ND2 ASN d 137 C1 NAG d 602 1555 1555 1.52 LINK ND2 ASN d 156 C1 NAG d 606 1555 1555 1.38 LINK ND2 ASN d 156 O5 NAG d 606 1555 1555 1.36 LINK ND2 ASN d 160 C1 NAG d 610 1555 1555 1.39 LINK ND2 ASN d 197 C1 NAG d 613 1555 1555 1.49 LINK ND2 ASN d 234 C1 NAG d 615 1555 1555 1.41 LINK ND2 ASN d 234 O5 NAG d 615 1555 1555 1.42 LINK ND2 ASN d 262 C1 NAG d 618 1555 1555 1.42 LINK ND2 ASN d 276 C1 NAG d 650 1555 1555 1.39 LINK ND2 ASN d 301 C1 NAG d 626 1555 1555 1.40 LINK ND2 ASN d 332 C1 NAG d 639 1555 1555 1.43 LINK ND2 ASN d 355 C1 NAG d 628 1555 1555 1.40 LINK ND2 ASN d 363 C1 NAG d 629 1555 1555 1.36 LINK ND2 ASN d 386 C1 NAG d 632 1555 1555 1.37 LINK ND2 ASN d 392 C1 NAG d 637 1555 1555 1.42 LINK ND2 ASN d 448 C1 NAG d 648 1555 1555 1.35 LINK O4 NAG C 602 C1 NAG C 603 1555 1555 1.44 LINK O4 NAG C 603 C1 BMA C 604 1555 1555 1.44 LINK O3 BMA C 604 C1 MAN C 605 1555 1555 1.44 LINK O4 NAG C 606 C1 NAG C 607 1555 1555 1.44 LINK O4 NAG C 607 C1 BMA C 608 1555 1555 1.45 LINK O3 BMA C 608 C1 MAN C 609 1555 1555 1.44 LINK O4 NAG C 610 C1 NAG C 611 1555 1555 1.43 LINK O4 NAG C 611 C1 BMA C 612 1555 1555 1.45 LINK O4 NAG C 613 C1 NAG C 614 1555 1555 1.45 LINK O4 NAG C 615 C1 NAG C 616 1555 1555 1.45 LINK O4 NAG C 616 C1 BMA C 617 1555 1555 1.44 LINK O4 NAG C 618 C1 NAG C 619 1555 1555 1.45 LINK O4 NAG C 619 C1 BMA C 620 1555 1555 1.44 LINK O3 BMA C 620 C1 MAN C 621 1555 1555 1.44 LINK O6 BMA C 620 C1 MAN C 622 1555 1555 1.45 LINK O2 MAN C 621 C1 MAN C 623 1555 1555 1.44 LINK O4 NAG C 624 C1 NAG C 625 1555 1555 1.45 LINK O4 NAG C 626 C1 NAG C 627 1555 1555 1.45 LINK O4 NAG C 629 C1 NAG C 630 1555 1555 1.43 LINK O4 NAG C 630 C1 BMA C 631 1555 1555 1.47 LINK O4 NAG C 632 C1 NAG C 633 1555 1555 1.44 LINK O4 NAG C 633 C1 BMA C 634 1555 1555 1.44 LINK O3 BMA C 634 C1 MAN C 635 1555 1555 1.44 LINK O6 BMA C 634 C1 MAN C 636 1555 1555 1.44 LINK O4 NAG C 637 C1 NAG C 638 1555 1555 1.46 LINK O4 NAG C 639 C1 NAG C 640 1555 1555 1.44 LINK O4 NAG C 640 C1 BMA C 641 1555 1555 1.44 LINK O3 BMA C 641 C1 MAN C 642 1555 1555 1.45 LINK O6 BMA C 641 C1 MAN C 643 1555 1555 1.44 LINK O2 MAN C 642 C1 MAN C 644 1555 1555 1.44 LINK O3 MAN C 643 C1 MAN C 645 1555 1555 1.44 LINK O6 MAN C 643 C1 MAN C 646 1555 1555 1.44 LINK O2 MAN C 644 C1 MAN C 647 1555 1555 1.43 LINK O4 NAG C 648 C1 NAG C 649 1555 1555 1.45 LINK O4 NAG C 650 C1 NAG C 651 1555 1555 1.43 LINK O4 NAG C 651 C1 BMA C 652 1555 1555 1.45 LINK O3 BMA C 652 C1 MAN C 653 1555 1555 1.45 LINK O4 NAG 2 602 C1 NAG 2 603 1555 1555 1.44 LINK O4 NAG 2 603 C1 BMA 2 604 1555 1555 1.44 LINK O3 BMA 2 604 C1 MAN 2 605 1555 1555 1.44 LINK O4 NAG 2 606 C1 NAG 2 607 1555 1555 1.45 LINK O4 NAG 2 607 C1 BMA 2 608 1555 1555 1.45 LINK O3 BMA 2 608 C1 MAN 2 609 1555 1555 1.44 LINK O4 NAG 2 610 C1 NAG 2 611 1555 1555 1.43 LINK O4 NAG 2 611 C1 BMA 2 612 1555 1555 1.45 LINK O4 NAG 2 613 C1 NAG 2 614 1555 1555 1.45 LINK O4 NAG 2 615 C1 NAG 2 616 1555 1555 1.45 LINK O4 NAG 2 616 C1 BMA 2 617 1555 1555 1.44 LINK O4 NAG 2 618 C1 NAG 2 619 1555 1555 1.45 LINK O4 NAG 2 619 C1 BMA 2 620 1555 1555 1.44 LINK O3 BMA 2 620 C1 MAN 2 621 1555 1555 1.44 LINK O6 BMA 2 620 C1 MAN 2 622 1555 1555 1.45 LINK O2 MAN 2 621 C1 MAN 2 623 1555 1555 1.44 LINK O4 NAG 2 624 C1 NAG 2 625 1555 1555 1.45 LINK O4 NAG 2 626 C1 NAG 2 627 1555 1555 1.45 LINK O4 NAG 2 629 C1 NAG 2 630 1555 1555 1.43 LINK O4 NAG 2 630 C1 BMA 2 631 1555 1555 1.47 LINK O4 NAG 2 632 C1 NAG 2 633 1555 1555 1.44 LINK O4 NAG 2 633 C1 BMA 2 634 1555 1555 1.44 LINK O3 BMA 2 634 C1 MAN 2 635 1555 1555 1.44 LINK O6 BMA 2 634 C1 MAN 2 636 1555 1555 1.44 LINK O4 NAG 2 637 C1 NAG 2 638 1555 1555 1.46 LINK O4 NAG 2 639 C1 NAG 2 640 1555 1555 1.44 LINK O4 NAG 2 640 C1 BMA 2 641 1555 1555 1.44 LINK O3 BMA 2 641 C1 MAN 2 642 1555 1555 1.45 LINK O6 BMA 2 641 C1 MAN 2 643 1555 1555 1.44 LINK O2 MAN 2 642 C1 MAN 2 644 1555 1555 1.44 LINK O3 MAN 2 643 C1 MAN 2 645 1555 1555 1.43 LINK O6 MAN 2 643 C1 MAN 2 646 1555 1555 1.44 LINK O2 MAN 2 644 C1 MAN 2 647 1555 1555 1.43 LINK O4 NAG 2 648 C1 NAG 2 649 1555 1555 1.45 LINK O4 NAG 2 650 C1 NAG 2 651 1555 1555 1.43 LINK O4 NAG 2 651 C1 BMA 2 652 1555 1555 1.45 LINK O3 BMA 2 652 C1 MAN 2 653 1555 1555 1.45 LINK O4 NAG d 602 C1 NAG d 603 1555 1555 1.44 LINK O4 NAG d 603 C1 BMA d 604 1555 1555 1.44 LINK O3 BMA d 604 C1 MAN d 605 1555 1555 1.44 LINK O4 NAG d 606 C1 NAG d 607 1555 1555 1.44 LINK O4 NAG d 607 C1 BMA d 608 1555 1555 1.45 LINK O3 BMA d 608 C1 MAN d 609 1555 1555 1.44 LINK O4 NAG d 610 C1 NAG d 611 1555 1555 1.43 LINK O4 NAG d 611 C1 BMA d 612 1555 1555 1.45 LINK O4 NAG d 613 C1 NAG d 614 1555 1555 1.45 LINK O4 NAG d 615 C1 NAG d 616 1555 1555 1.45 LINK O4 NAG d 616 C1 BMA d 617 1555 1555 1.44 LINK O4 NAG d 618 C1 NAG d 619 1555 1555 1.45 LINK O4 NAG d 619 C1 BMA d 620 1555 1555 1.44 LINK O3 BMA d 620 C1 MAN d 621 1555 1555 1.44 LINK O6 BMA d 620 C1 MAN d 622 1555 1555 1.45 LINK O2 MAN d 621 C1 MAN d 623 1555 1555 1.44 LINK O4 NAG d 624 C1 NAG d 625 1555 1555 1.45 LINK O4 NAG d 626 C1 NAG d 627 1555 1555 1.45 LINK O4 NAG d 629 C1 NAG d 630 1555 1555 1.43 LINK O4 NAG d 630 C1 BMA d 631 1555 1555 1.47 LINK O4 NAG d 632 C1 NAG d 633 1555 1555 1.44 LINK O4 NAG d 633 C1 BMA d 634 1555 1555 1.44 LINK O3 BMA d 634 C1 MAN d 635 1555 1555 1.44 LINK O6 BMA d 634 C1 MAN d 636 1555 1555 1.44 LINK O4 NAG d 637 C1 NAG d 638 1555 1555 1.46 LINK O4 NAG d 639 C1 NAG d 640 1555 1555 1.44 LINK O4 NAG d 640 C1 BMA d 641 1555 1555 1.44 LINK O3 BMA d 641 C1 MAN d 642 1555 1555 1.45 LINK O6 BMA d 641 C1 MAN d 643 1555 1555 1.44 LINK O2 MAN d 642 C1 MAN d 644 1555 1555 1.44 LINK O3 MAN d 643 C1 MAN d 645 1555 1555 1.44 LINK O6 MAN d 643 C1 MAN d 646 1555 1555 1.44 LINK O2 MAN d 644 C1 MAN d 647 1555 1555 1.43 LINK O4 NAG d 648 C1 NAG d 649 1555 1555 1.45 LINK O4 NAG d 650 C1 NAG d 651 1555 1555 1.43 LINK O4 NAG d 651 C1 BMA d 652 1555 1555 1.45 LINK O3 BMA d 652 C1 MAN d 653 1555 1555 1.45 CISPEP 1 THR 4 7 PRO 4 8 0 2.77 CISPEP 2 VAL 4 99 PRO 4 100 0 -1.48 CISPEP 3 THR L 7 PRO L 8 0 2.79 CISPEP 4 VAL L 99 PRO L 100 0 -1.62 CISPEP 5 THR l 7 PRO l 8 0 2.23 CISPEP 6 VAL l 99 PRO l 100 0 -3.17 SITE 1 AC1 2 ASN 2 133 ARG 2 178 SITE 1 AC2 2 ASN 2 133 ARG 2 178 SITE 1 AC3 6 ASN 2 137 ASN 5 58 PHE 5 100K THR 5 100L SITE 2 AC3 6 ASP 6 92 THR 6 95B SITE 1 AC4 5 VAL 2 134 THR 2 135 ASN 2 156 TYR 2 173 SITE 2 AC4 5 ASP 2 321A SITE 1 AC5 5 GLN 2 130 SER 2 158 ASN 2 160 LYS 2 169 SITE 2 AC5 5 LYS 2 171 SITE 1 AC6 5 ARG 2 192 ASN 2 197 THR 2 198 GLN 8 75 SITE 2 AC6 5 ARG C 308 SITE 1 AC7 3 ASN 2 234 GLU 2 275 ILE 2 277 SITE 1 AC8 6 SER 2 209 ASN 2 262 ARG 2 304 ASN 2 377 SITE 2 AC8 6 GLY 2 379 SER 2 447 SITE 1 AC9 6 ASN 2 94 LYS 2 97 ASN 2 276 ALA 7 32 SITE 2 AC9 6 ASP 7 50 PHE 7 91 SITE 1 AD1 2 ASN 2 301 ILE 2 323 SITE 1 AD2 13 ASN 2 295 HIS 2 330 ASN 2 332 SER 2 413 SITE 2 AD2 13 ARG 5 100 ILE 5 100A GLY 5 100C ASN 6 50 SITE 3 AD2 13 ASN 6 51 ASN 6 52 PRO 6 66 GLY 6 67 SITE 4 AD2 13 SER 6 67A SITE 1 AD3 2 LYS 2 347 ASN 2 355 SITE 1 AD4 5 ASN 2 363 SER 2 364 SER 2 388 NAG 2 632 SITE 2 AD4 5 NAG 2 633 SITE 1 AD5 5 ASN 2 386 SER 2 388 NAG 2 629 NAG 2 630 SITE 2 AD5 5 NAG 2 637 SITE 1 AD6 3 ASN 2 392 NAG 2 632 NAG 2 633 SITE 1 AD7 1 ASN 2 448 SITE 1 AD8 1 ASN A 637 SITE 1 AD9 2 ASN C 133 ARG C 178 SITE 1 AE1 2 ASN C 133 ARG C 178 SITE 1 AE2 6 ASN C 137 GLY M 55 ASN M 58 THR M 100L SITE 2 AE2 6 ASP N 92 THR N 95B SITE 1 AE3 5 VAL C 134 ASN C 156 TYR C 173 LEU C 175 SITE 2 AE3 5 ASP C 321A SITE 1 AE4 5 GLN C 130 SER C 158 ASN C 160 LYS C 169 SITE 2 AE4 5 LYS C 171 SITE 1 AE5 5 ARG C 192 ASN C 197 THR C 198 GLN Q 75 SITE 2 AE5 5 ARG d 308 SITE 1 AE6 3 ASN C 234 GLU C 275 ILE C 277 SITE 1 AE7 6 SER C 209 ASN C 262 ARG C 304 ASN C 377 SITE 2 AE7 6 GLY C 379 SER C 447 SITE 1 AE8 6 ASN C 94 LYS C 97 ASN C 276 ALA R 32 SITE 2 AE8 6 ASP R 50 PHE R 91 SITE 1 AE9 2 ASN C 301 ILE C 323 SITE 1 AF1 13 ASN C 295 HIS C 330 ASN C 332 SER C 413 SITE 2 AF1 13 ARG M 100 ILE M 100A GLY M 100C ASN N 50 SITE 3 AF1 13 ASN N 51 ASN N 52 PRO N 66 GLY N 67 SITE 4 AF1 13 SER N 67A SITE 1 AF2 2 LYS C 347 ASN C 355 SITE 1 AF3 5 ASN C 363 SER C 364 SER C 388 NAG C 632 SITE 2 AF3 5 NAG C 633 SITE 1 AF4 5 ASN C 386 SER C 388 NAG C 629 NAG C 630 SITE 2 AF4 5 NAG C 637 SITE 1 AF5 3 ASN C 392 NAG C 632 NAG C 633 SITE 1 AF6 1 ASN C 448 SITE 1 AF7 1 ASN D 637 SITE 1 AF8 1 ASN c 637 SITE 1 AF9 2 ASN d 133 ARG d 178 SITE 1 AG1 2 ASN d 133 ARG d 178 SITE 1 AG2 6 ASN d 137 GLY m 55 ASN m 58 THR m 100L SITE 2 AG2 6 ASP n 92 THR n 95B SITE 1 AG3 5 VAL d 134 THR d 135 ASN d 156 TYR d 173 SITE 2 AG3 5 ASP d 321A SITE 1 AG4 5 GLN d 130 SER d 158 ASN d 160 LYS d 169 SITE 2 AG4 5 LYS d 171 SITE 1 AG5 5 ARG 2 308 ARG d 192 ASN d 197 THR d 198 SITE 2 AG5 5 GLN q 75 SITE 1 AG6 3 ASN d 234 GLU d 275 ILE d 277 SITE 1 AG7 6 SER d 209 ASN d 262 ARG d 304 ASN d 377 SITE 2 AG7 6 GLY d 379 SER d 447 SITE 1 AG8 6 ASN d 94 LYS d 97 ASN d 276 ALA r 32 SITE 2 AG8 6 ASP r 50 PHE r 91 SITE 1 AG9 2 ASN d 301 ILE d 323 SITE 1 AH1 13 ASN d 295 HIS d 330 ASN d 332 SER d 413 SITE 2 AH1 13 ARG m 100 ILE m 100A GLY m 100C ASN n 50 SITE 3 AH1 13 ASN n 51 ASN n 52 PRO n 66 GLY n 67 SITE 4 AH1 13 SER n 67A SITE 1 AH2 2 LYS d 347 ASN d 355 SITE 1 AH3 5 ASN d 363 SER d 364 SER d 388 NAG d 632 SITE 2 AH3 5 NAG d 633 SITE 1 AH4 5 ASN d 386 SER d 388 NAG d 629 NAG d 630 SITE 2 AH4 5 NAG d 637 SITE 1 AH5 3 ASN d 392 NAG d 632 NAG d 633 SITE 1 AH6 1 ASN d 448 SITE 1 AH7 3 GLN 2 293 ASN 2 295 SER 2 334 SITE 1 AH8 3 GLN C 293 ASN C 295 SER C 334 SITE 1 AH9 3 GLN d 293 ASN d 295 SER d 334 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000